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Created November 8, 2022 20:23
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<skos:narrowerTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.409"/>
<skos:narrowerTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.410"/>
<skos:narrowerTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.411"/>
<skos:narrowerTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.412"/>
<skos:narrowerTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.413"/>
<skos:narrowerTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.414"/>
<skos:narrowerTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.415"/>
<skos:narrowerTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.416"/>
<skos:narrowerTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.417"/>
<skos:narrowerTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.418"/>
<skos:narrowerTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.419"/>
<skos:narrowerTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.420"/>
<skos:narrowerTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.421"/>
<skos:narrowerTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.422"/>
<skos:narrowerTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.423"/>
<skos:narrowerTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.424"/>
<skos:narrowerTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.425"/>
<skos:narrowerTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.426"/>
<skos:narrowerTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.427"/>
<skos:narrowerTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.428"/>
<skos:narrowerTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.429"/>
<skos:narrowerTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.n4"/>
<skos:narrowerTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.n5"/>
<skos:narrowerTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.n11"/>
<skos:narrowerTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.n12"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.1">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>alcohol dehydrogenase</skos:prefLabel>
<skos:altLabel>aldehyde reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.1#SIP8826B9F272890D4B"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.1#SIP6397FC79E265D1A2"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.1#SIPCBE86A7B154A6E37"/>
<rdfs:comment>Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol.</rdfs:comment>
<rdfs:comment>The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/320001"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.1#SIP8826B9F272890D4B">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.1#SIP6397FC79E265D1A2">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>a secondary alcohol + NAD(+) = a ketone + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.1#SIPCBE86A7B154A6E37">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>ethanol + NAD(+) = acetaldehyde + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/320001">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/320001"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/320001"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.2">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>alcohol dehydrogenase (NADP(+))</skos:prefLabel>
<skos:altLabel>aldehyde reductase (NADPH)</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.2#SIP85407D6214AA0FCB"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.2#SIPD3F01639DC45DCBC"/>
<rdfs:comment>Some members of this group oxidize only primary alcohols; others act also on secondary alcohols.</rdfs:comment>
<rdfs:comment>May be identical with EC 1.1.1.19, EC 1.1.1.33 and EC 1.1.1.55.</rdfs:comment>
<rdfs:comment>Re-specific with respect to NADPH.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/4393513"/>
<citation rdf:resource="http://purl.uniprot.org/citations/4402936"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.2#SIP85407D6214AA0FCB">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>a primary alcohol + NADP(+) = an aldehyde + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.2#SIPD3F01639DC45DCBC">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>a secondary alcohol + NADP(+) = a ketone + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/4393513">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/4393513"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/4393513"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/4402936">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/4402936"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/4402936"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.3">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>homoserine dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.3#SIPDA9B175EA7C069C1"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.3#SIP8871D40C4AE199A9"/>
<rdfs:comment>The enzyme from Saccharomyces cerevisiae acts most rapidly with NAD(+); the Neurospora enzyme with NADP(+).</rdfs:comment>
<rdfs:comment>The enzyme from Escherichia coli is a multifunctional protein, which also catalyzes the reaction of EC 2.7.2.4.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/4551091"/>
<citation rdf:resource="http://purl.uniprot.org/citations/4562990"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.3#SIPDA9B175EA7C069C1">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.3#SIP8871D40C4AE199A9">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>L-homoserine + NADP(+) = H(+) + L-aspartate 4-semialdehyde + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/4551091">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/4551091"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/4551091"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/4562990">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/4562990"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/4562990"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.4">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>(R,R)-butanediol dehydrogenase</skos:prefLabel>
<skos:altLabel>(R)-2,3-butanediol dehydrogenase</skos:altLabel>
<skos:altLabel>(R)-diacetyl reductase</skos:altLabel>
<skos:altLabel>1-amino-2-propanol dehydrogenase</skos:altLabel>
<skos:altLabel>1-amino-2-propanol oxidoreductase</skos:altLabel>
<skos:altLabel>2,3-butanediol dehydrogenase</skos:altLabel>
<skos:altLabel>aminopropanol oxidoreductase</skos:altLabel>
<skos:altLabel>butyleneglycol dehydrogenase</skos:altLabel>
<skos:altLabel>butylene glycol dehydrogenase</skos:altLabel>
<skos:altLabel>D-(-)-butanediol dehydrogenase</skos:altLabel>
<skos:altLabel>D-1-amino-2-propanol:NAD(2) oxidoreductase</skos:altLabel>
<skos:altLabel>D-1-amino-2-propanol dehydrogenase</skos:altLabel>
<skos:altLabel>D-aminopropanol dehydrogenase</skos:altLabel>
<skos:altLabel>D-butanediol dehydrogenase</skos:altLabel>
<skos:altLabel>diacetyl (acetoin) reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.4#SIP76FB16551FDA8FEC"/>
<rdfs:comment>Also converts diacetyl into acetoin with NADH as reductant.</rdfs:comment>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.4#SIP76FB16551FDA8FEC">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(R,R)-butane-2,3-diol + NAD(+) = (R)-acetoin + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.5">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<obsolete rdf:datatype="http://www.w3.org/2001/XMLSchema#boolean">true</obsolete>
<replacedBy rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.303"/>
<replacedBy rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.304"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.6">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>glycerol dehydrogenase</skos:prefLabel>
<skos:altLabel>NAD-linked glycerol dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.6#SIP528B03D21D5CFFDA"/>
<rdfs:comment>Also acts on 1,2-propanediol.</rdfs:comment>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.6#SIP528B03D21D5CFFDA">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>glycerol + NAD(+) = dihydroxyacetone + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.7">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>propanediol-phosphate dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.7#SIP73AB11FF72A444D7"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.7#SIP73AB11FF72A444D7">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>NAD(+) + propane-1,2-diol 1-phosphate = H(+) + hydroxyacetone phosphate + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.8">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>glycerol-3-phosphate dehydrogenase (NAD(+))</skos:prefLabel>
<skos:altLabel>alpha-glycerol phosphate dehydrogenase (NAD)</skos:altLabel>
<skos:altLabel>alpha-glycerophosphate dehydrogenase (NAD)</skos:altLabel>
<skos:altLabel>glycerol 1-phosphate dehydrogenase</skos:altLabel>
<skos:altLabel>glycerol-3-phosphate dehydrogenase (NAD)</skos:altLabel>
<skos:altLabel>glycerol phosphate dehydrogenase (NAD)</skos:altLabel>
<skos:altLabel>glycerophosphate dehydrogenase (NAD)</skos:altLabel>
<skos:altLabel>hydroglycerophosphate dehydrogenase</skos:altLabel>
<skos:altLabel>L-alpha-glycerol phosphate dehydrogenase</skos:altLabel>
<skos:altLabel>L-alpha-glycerophosphate dehydrogenase</skos:altLabel>
<skos:altLabel>L-glycerol-3-phosphate dehydrogenase</skos:altLabel>
<skos:altLabel>L-glycerol phosphate dehydrogenase</skos:altLabel>
<skos:altLabel>L-glycerophosphate dehydrogenase</skos:altLabel>
<skos:altLabel>NAD-alpha-glycerophosphate dehydrogenase</skos:altLabel>
<skos:altLabel>NAD-dependent glycerol-3-phosphate dehydrogenase</skos:altLabel>
<skos:altLabel>NAD-dependent glycerol phosphate dehydrogenase</skos:altLabel>
<skos:altLabel>NADH-dihydroxyacetone phosphate reductase</skos:altLabel>
<skos:altLabel>NAD-L-glycerol-3-phosphate dehydrogenase</skos:altLabel>
<skos:altLabel>NAD-linked glycerol 3-phosphate dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.8#SIPE0E68CB842BFB643"/>
<rdfs:comment>Also acts on propane-1,2-diol phosphate and glycerone sulfate (but with a much lower affinity).</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/1499720"/>
<citation rdf:resource="http://purl.uniprot.org/citations/4200180"/>
<citation rdf:resource="http://purl.uniprot.org/citations/4307630"/>
<citation rdf:resource="http://purl.uniprot.org/citations/4340553"/>
<citation rdf:resource="http://purl.uniprot.org/citations/7671141"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.8#SIPE0E68CB842BFB643">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/1499720">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/1499720"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/1499720"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/4200180">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/4200180"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/4307630">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/4307630"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/4307630"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/4340553">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/4340553"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/4340553"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/7671141">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/7671141"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/7671141"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.9">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>D-xylulose reductase</skos:prefLabel>
<skos:altLabel>xylitol dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.9#SIP6C7151AFBA233343"/>
<rdfs:comment>Also acts as an L-erythrulose reductase.</rdfs:comment>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.9#SIP6C7151AFBA233343">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>NAD(+) + xylitol = D-xylulose + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.10">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>L-xylulose reductase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.10#SIP37999F3468BC57BC"/>
<citation rdf:resource="http://purl.uniprot.org/citations/2981816"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.10#SIP37999F3468BC57BC">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>NADP(+) + xylitol = H(+) + L-xylulose + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/2981816">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/2981816"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/2981816"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.11">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>D-arabinitol 4-dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.11#SIP9DCDC2FD240FA880"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.11#SIP9DCDC2FD240FA880">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-arabinitol + NAD(+) = D-xylulose + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.12">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>L-arabinitol 4-dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.12#SIPAE122BC406B6D006"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.12#SIPAE122BC406B6D006">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>L-arabinitol + NAD(+) = H(+) + L-xylulose + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.13">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>L-arabinitol 2-dehydrogenase</skos:prefLabel>
<skos:altLabel>L-arabinitol 2-dehydrogenase (ribulose forming)</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.13#SIPDC750E3E3D30C425"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.13#SIPDC750E3E3D30C425">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>L-arabinitol + NAD(+) = H(+) + L-ribulose + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.14">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>L-iditol 2-dehydrogenase</skos:prefLabel>
<skos:altLabel>glucitol dehydrogenase</skos:altLabel>
<skos:altLabel>polyol dehydrogenase</skos:altLabel>
<skos:altLabel>sorbitol dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.14#SIPD00AE08C710FA4C0"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.14#SIPADAFEE143732680A"/>
<rdfs:comment>This enzyme is widely distributed and has been described in archaea, bacteria, yeast, plants and animals.</rdfs:comment>
<rdfs:comment>It acts on a number of sugar alcohols, including (but not limited to) L-iditol, D-glucitol, D-xylitol, and D-galactitol.</rdfs:comment>
<rdfs:comment>Enzymes from different organisms or tissues display different substrate specificity.</rdfs:comment>
<rdfs:comment>The enzyme is specific to NAD(+) and can not use NADP(+).</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/667078"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.14#SIPD00AE08C710FA4C0">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>L-iditol + NAD(+) = H(+) + keto-L-sorbose + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.14#SIPADAFEE143732680A">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>H(+) + keto-D-fructose + NADH = D-sorbitol + NAD(+).</rdfs:label>
</rdf:Description>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.15">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>D-iditol 2-dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.15#SIP05AEFFEC26662B9E"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.15#SIPECB98051BFD3696B"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.15#SIP0A29B2F3E5B34D8C"/>
<rdfs:comment>Also converts xylitol into L-xylulose and L-glucitol into L-fructose.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/13373783"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.15#SIP05AEFFEC26662B9E">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-iditol + NAD(+) = H(+) + keto-D-sorbose + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.15#SIPECB98051BFD3696B">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>NAD(+) + xylitol = H(+) + L-xylulose + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.15#SIP0A29B2F3E5B34D8C">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>L-glucitol + NAD(+) = H(+) + keto-L-fructose + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/13373783">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/13373783"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/13373783"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.16">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>galactitol 2-dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.16#SIPE1B1F7E810F8AC53"/>
<rdfs:comment>Also converts other alditols containing an L-threo-configuration adjacent to a primary alcohol group into the corresponding sugars.</rdfs:comment>
<rdfs:comment>The enzyme from Agrobacterium rubrum C58 is part of D-altritol and galactitol degradation pathways.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/26472925"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.16#SIPE1B1F7E810F8AC53">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>galactitol + NAD(+) = H(+) + keto-D-tagatose + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/26472925">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/26472925"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/26472925"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.17">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>mannitol-1-phosphate 5-dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.17#SIP0F63717883600433"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.17#SIP0F63717883600433">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-mannitol 1-phosphate + NAD(+) = beta-D-fructose 6-phosphate + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.18">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>inositol 2-dehydrogenase</skos:prefLabel>
<skos:altLabel>myo-inositol 2-dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.18#SIP19C57E45AC5456AA"/>
<citation rdf:resource="http://purl.uniprot.org/citations/4351258"/>
<citation rdf:resource="http://purl.uniprot.org/citations/5905122"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.18#SIP19C57E45AC5456AA">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>myo-inositol + NAD(+) = H(+) + NADH + scyllo-inosose.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/4351258">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/4351258"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/5905122">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/5905122"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/5905122"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.19">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>glucuronate reductase</skos:prefLabel>
<skos:altLabel>D-glucuronate dehydrogenase</skos:altLabel>
<skos:altLabel>D-glucuronate reductase</skos:altLabel>
<skos:altLabel>glucuronate dehydrogenase</skos:altLabel>
<skos:altLabel>L-glucuronate reductase</skos:altLabel>
<skos:altLabel>NADP-L-gulonate dehydrogenase</skos:altLabel>
<skos:altLabel>TPN-L-gulonate dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.19#SIP8656FA3E453DB495"/>
<rdfs:comment>Also reduces D-galacturonate.</rdfs:comment>
<rdfs:comment>May be identical with EC 1.1.1.2.</rdfs:comment>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.19#SIP8656FA3E453DB495">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>L-gulonate + NADP(+) = aldehydo-D-glucuronate + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.20">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>glucuronolactone reductase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.20#SIPBAC327F7BF424E88"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.20#SIPBAC327F7BF424E88">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>L-gulono-1,4-lactone + NADP(+) = D-glucurono-3,6-lactone + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.21">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<replaces rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.139"/>
<skos:prefLabel>aldose reductase</skos:prefLabel>
<skos:altLabel>aldehyde reductase</skos:altLabel>
<skos:altLabel>polyol dehydrogenase (NADP(+))</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.21#SIP344FE83FF23DE88A"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.21#SIPE788E27CBE9A3278"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.21#SIP05DD6AEEDBC6685D"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.21#SIP35F62C95F5662209"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.21#SIP485AAFEDA74632EB"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.21#SIP54C28078C51C170E"/>
<rdfs:comment>Wide specificity.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/36151"/>
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<citation rdf:resource="http://purl.uniprot.org/citations/4381350"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.21#SIP344FE83FF23DE88A">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>an alditol + NAD(+) = an aldose + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.21#SIPE788E27CBE9A3278">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>an alditol + NADP(+) = an aldose + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.21#SIP05DD6AEEDBC6685D">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>galactitol + NADP(+) = D-galactose + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.21#SIP35F62C95F5662209">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>galactitol + NAD(+) = D-galactose + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.21#SIP485AAFEDA74632EB">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>L-arabinitol + NAD(+) = H(+) + L-arabinose + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.21#SIP54C28078C51C170E">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>L-arabinitol + NADP(+) = H(+) + L-arabinose + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/36151">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/4216364">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/4216364"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/citations/4381350">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
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<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/4381350"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.22">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>UDP-glucose 6-dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.22#SIPF28F1A915D39D5B8"/>
<rdfs:comment>Also acts on UDP-2-deoxyglucose.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/1091296"/>
<citation rdf:resource="http://purl.uniprot.org/citations/13373402"/>
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<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.22#SIPF28F1A915D39D5B8">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate.</rdfs:label>
</rdf:Description>
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<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/13459898"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.23">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>histidinol dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.23#SIP115A23E2779EDA82"/>
<rdfs:comment>Also oxidizes L-histidinal.</rdfs:comment>
<rdfs:comment>The Neurospora enzyme also catalyzes the reactions of EC 3.5.4.19 and EC 3.6.1.31.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/4872176"/>
<citation rdf:resource="http://purl.uniprot.org/citations/4872177"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.23#SIP115A23E2779EDA82">
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<rdfs:label>H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH.</rdfs:label>
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<skos:prefLabel>quinate/shikimate dehydrogenase (NAD(+))</skos:prefLabel>
<skos:altLabel>quinate 5-dehydrogenase</skos:altLabel>
<skos:altLabel>quinate dehydrogenase</skos:altLabel>
<skos:altLabel>quinic dehydrogenase</skos:altLabel>
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<rdfs:comment>The enzyme, found mostly in bacteria (mostly, but not exclusively in Gram-positive bacteria), fungi, and plants, participates in the degradation of quinate and shikimate with a strong preference for NAD(+) as a cofactor.</rdfs:comment>
<rdfs:comment>While the enzyme can act on both quinate and shikimate, activity is higher with the former.</rdfs:comment>
<rdfs:comment>Cf. EC 1.1.1.25, EC 1.1.1.282, and EC 1.1.5.8.</rdfs:comment>
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<rdfs:label>L-quinate + NAD(+) = 3-dehydroquinate + H(+) + NADH.</rdfs:label>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.25">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>shikimate dehydrogenase (NADP(+))</skos:prefLabel>
<skos:altLabel>5-dehydroshikimate reductase</skos:altLabel>
<skos:altLabel>5-dehydroshikimic reductase</skos:altLabel>
<skos:altLabel>dehydroshikimic reductase</skos:altLabel>
<skos:altLabel>DHS reductase</skos:altLabel>
<skos:altLabel>shikimate 5-dehydrogenase</skos:altLabel>
<skos:altLabel>shikimate dehydrogenase</skos:altLabel>
<skos:altLabel>shikimate oxidoreductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.25#SIPCE4402C52A57D828"/>
<rdfs:comment>NAD(+) cannot replace NADP(+).</rdfs:comment>
<rdfs:comment>In higher organisms, this enzyme forms part of a multienzyme complex with EC 4.2.1.10.</rdfs:comment>
<rdfs:comment>Cf. EC 1.1.1.24, EC 1.1.1.282, and EC 1.1.5.8.</rdfs:comment>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.25#SIPCE4402C52A57D828">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.26">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>glyoxylate reductase</skos:prefLabel>
<skos:altLabel>glycolate reductase</skos:altLabel>
<skos:altLabel>glyoxylic acid reductase</skos:altLabel>
<skos:altLabel>NADH-dependent glyoxylate reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.26#SIP780D379ABC1B785C"/>
<rdfs:comment>Reduces glyoxylate to glycolate or hydroxypyruvate to D-glycerate.</rdfs:comment>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.26#SIP780D379ABC1B785C">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>glycolate + NAD(+) = glyoxylate + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.27">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>L-lactate dehydrogenase</skos:prefLabel>
<skos:altLabel>L-lactic acid dehydrogenase</skos:altLabel>
<skos:altLabel>L-lactic dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.27#SIP4F8E7F28225F5225"/>
<rdfs:comment>Also oxidizes other (S)-2-hydroxymonocarboxylic acids.</rdfs:comment>
<rdfs:comment>NADP(+) acts, more slowly, with the animal, but not the bacterial, enzyme.</rdfs:comment>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.27#SIP4F8E7F28225F5225">
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<rdfs:label>(S)-lactate + NAD(+) = H(+) + NADH + pyruvate.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.28">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>D-lactate dehydrogenase</skos:prefLabel>
<skos:altLabel>D-lactic acid dehydrogenase</skos:altLabel>
<skos:altLabel>D-lactic dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.28#SIP4ED419B0A422B7DD"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.28#SIP4ED419B0A422B7DD">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(R)-lactate + NAD(+) = H(+) + NADH + pyruvate.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.29">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>glycerate dehydrogenase</skos:prefLabel>
<skos:altLabel>D-glycerate dehydrogenase</skos:altLabel>
<skos:altLabel>hydroxypyruvate dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.29#SIP2D29B6D762CA3AC1"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.29#SIP2D29B6D762CA3AC1">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(R)-glycerate + NAD(+) = 3-hydroxypyruvate + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.30">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>3-hydroxybutyrate dehydrogenase</skos:prefLabel>
<skos:altLabel>D-beta-hydroxybutyrate dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.30#SIP8F44155BD05CFB5B"/>
<rdfs:comment>Also oxidizes other 3-hydroxymonocarboxylic acids.</rdfs:comment>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.30#SIP8F44155BD05CFB5B">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(R)-3-hydroxybutanoate + NAD(+) = acetoacetate + H(+) + NADH.</rdfs:label>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.31">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>3-hydroxyisobutyrate dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.31#SIPB9FAD79A97F792EC"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.31#SIP027B4FF1D8C50154"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.31#SIPB9FAD79A97F792EC">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>3-hydroxy-2-methylpropanoate + NAD(+) = 2-methyl-3-oxopropanoate + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.31#SIP027B4FF1D8C50154">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(S)-3-hydroxy-2-methylpropanoate + NAD(+) = (S)-methylmalonate semialdehyde + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.32">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>mevaldate reductase</skos:prefLabel>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.32#SIP6DA545E60958FE37">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(R)-mevalonate + NAD(+) = H(+) + mevaldate + NADH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.33">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>mevaldate reductase (NADPH)</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.33#SIP707085ABAE9D3CED"/>
<rdfs:comment>May be identical with EC 1.1.1.2.</rdfs:comment>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(R)-mevalonate + NADP(+) = H(+) + mevaldate + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.34">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>hydroxymethylglutaryl-CoA reductase (NADPH)</skos:prefLabel>
<skos:altLabel>3-hydroxy-3-methylglutaryl-coenzyme A reductase</skos:altLabel>
<skos:altLabel>HMG-CoA reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.34#SIP5E174D49A8BB9028"/>
<rdfs:comment>The enzyme is inactivated by EC 2.7.11.31 and reactivated by EC 3.1.3.47.</rdfs:comment>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.34#SIP5E174D49A8BB9028">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADPH.</rdfs:label>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.35">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>3-hydroxyacyl-CoA dehydrogenase</skos:prefLabel>
<skos:altLabel>beta-hydroxyacyl dehydrogenase</skos:altLabel>
<skos:altLabel>beta-keto-reductase</skos:altLabel>
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<rdfs:comment>Also oxidizes S-3-hydroxyacyl-N-acylthioethanolamine and S-3-hydroxyacylhydrolipoate.</rdfs:comment>
<rdfs:comment>Some enzymes act, more slowly, with NADP(+).</rdfs:comment>
<rdfs:comment>Broad specificity to acyl chain-length (cf. EC 1.1.1.211).</rdfs:comment>
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<rdfs:label>a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH.</rdfs:label>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>acetoacetyl-CoA reductase</skos:prefLabel>
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<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.36#SIP11F9B69CE946F8E5"/>
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<rdfs:label>a (3R)-3-hydroxyacyl-CoA + NADP(+) = a 3-oxoacyl-CoA + H(+) + NADPH.</rdfs:label>
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<rdfs:label>(3R)-3-hydroxybutanoyl-CoA + NADP(+) = acetoacetyl-CoA + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.37">
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<skos:prefLabel>malate dehydrogenase</skos:prefLabel>
<skos:altLabel>malic dehydrogenase</skos:altLabel>
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<rdfs:comment>Also oxidizes some other 2-hydroxydicarboxylic acids.</rdfs:comment>
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<rdfs:label>(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate.</rdfs:label>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>malate dehydrogenase (oxaloacetate-decarboxylating)</skos:prefLabel>
<skos:altLabel>malic enzyme</skos:altLabel>
<skos:altLabel>NAD-malic enzyme</skos:altLabel>
<skos:altLabel>pyruvic-malic carboxylase</skos:altLabel>
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<rdfs:comment>Unlike EC 1.1.1.39, this enzyme can also decarboxylate oxaloacetate, cf. EC 1.1.1.40.</rdfs:comment>
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<rdfs:label>(S)-malate + NAD(+) = CO2 + NADH + pyruvate.</rdfs:label>
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<rdfs:label>H(+) + oxaloacetate = CO2 + pyruvate.</rdfs:label>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.39">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>malate dehydrogenase (decarboxylating)</skos:prefLabel>
<skos:altLabel>Malic enzyme</skos:altLabel>
<skos:altLabel>NAD-malic enzyme</skos:altLabel>
<skos:altLabel>pyruvic-malic carboxylase</skos:altLabel>
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<rdfs:comment>Does not decarboxylate added oxaloacetate.</rdfs:comment>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.39#SIP67CA97566F88E99B">
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<rdfs:label>(S)-malate + NAD(+) = CO2 + NADH + pyruvate.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.40">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>malate dehydrogenase (oxaloacetate-decarboxylating) (NADP(+))</skos:prefLabel>
<skos:altLabel>malic enzyme</skos:altLabel>
<skos:altLabel>NADP-malic enzyme</skos:altLabel>
<skos:altLabel>pyruvic-malic carboxylase</skos:altLabel>
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<rdfs:comment>The enzyme catalyzes the oxidative decarboxylation of (S)-malate in the presence of NADP(+) and divalent metal ions, and decarboxylation of oxaloacetate, cf. EC 1.1.1.38 and EC 1.1.1.39.</rdfs:comment>
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<rdfs:label>(S)-malate + NADP(+) = CO2 + NADPH + pyruvate.</rdfs:label>
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<rdfs:label>H(+) + oxaloacetate = CO2 + pyruvate.</rdfs:label>
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<skos:prefLabel>isocitrate dehydrogenase (NAD(+))</skos:prefLabel>
<skos:altLabel>beta-ketoglutaric-isocitric carboxylase</skos:altLabel>
<skos:altLabel>IDH</skos:altLabel>
<skos:altLabel>isocitrate dehydrogenase (NAD)</skos:altLabel>
<skos:altLabel>isocitric acid dehydrogenase</skos:altLabel>
<skos:altLabel>isocitric dehydrogenase</skos:altLabel>
<skos:altLabel>NAD dependent isocitrate dehydrogenase</skos:altLabel>
<skos:altLabel>NAD isocitrate dehydrogenase</skos:altLabel>
<skos:altLabel>NAD isocitric dehydrogenase</skos:altLabel>
<skos:altLabel>NAD-linked isocitrate dehydrogenase</skos:altLabel>
<skos:altLabel>NAD-specific isocitrate dehydrogenase</skos:altLabel>
<skos:altLabel>nicotinamide adenine dinucleotide isocitrate dehydrogenase</skos:altLabel>
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<rdfs:comment>Unlike EC 1.1.1.42, oxalosuccinate cannot be used as a substrate.</rdfs:comment>
<rdfs:comment>In eukaryotes, isocitrate dehydrogenase exists in two forms: an NAD(+)-linked enzyme found only in mitochondria and displaying allosteric properties, and a non-allosteric, NADP(+)-linked enzyme that is found in both mitochondria and cytoplasm.</rdfs:comment>
<rdfs:comment>The enzyme from some species can also use NADP(+) but much more slowly.</rdfs:comment>
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<rdfs:label>D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH.</rdfs:label>
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<skos:prefLabel>isocitrate dehydrogenase (NADP(+))</skos:prefLabel>
<skos:altLabel>dual-cofactor-specific isocitrate dehydrogenase</skos:altLabel>
<skos:altLabel>IDH</skos:altLabel>
<skos:altLabel>IDP</skos:altLabel>
<skos:altLabel>isocitrate (NADP) dehydrogenase</skos:altLabel>
<skos:altLabel>isocitrate (nicotinamide adenine dinucleotide phosphate) dehydrogenase</skos:altLabel>
<skos:altLabel>isocitrate dehydrogenase (NADP)</skos:altLabel>
<skos:altLabel>isocitrate dehydrogenase (NADP-dependent)</skos:altLabel>
<skos:altLabel>NADP(+)-ICDH</skos:altLabel>
<skos:altLabel>NADP(+)-IDH</skos:altLabel>
<skos:altLabel>NADP(+)-linked isocitrate dehydrogenase</skos:altLabel>
<skos:altLabel>NADP-dependent isocitrate dehydrogenase</skos:altLabel>
<skos:altLabel>NADP-dependent isocitric dehydrogenase</skos:altLabel>
<skos:altLabel>NADP isocitric dehydrogenase</skos:altLabel>
<skos:altLabel>NADP-linked isocitrate dehydrogenase</skos:altLabel>
<skos:altLabel>NADP-specific isocitrate dehydrogenase</skos:altLabel>
<skos:altLabel>oxalosuccinate decarboxylase</skos:altLabel>
<skos:altLabel>oxalsuccinic decarboxylase</skos:altLabel>
<skos:altLabel>triphosphopyridine nucleotide-linked isocitrate dehydrogenase-oxalosuccinate carboxylase</skos:altLabel>
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<rdfs:comment>Unlike EC 1.1.1.41, oxalosuccinate can be used as a substrate.</rdfs:comment>
<rdfs:comment>In eukaryotes, isocitrate dehydrogenase exists in two forms: an NAD(+)-linked enzyme found only in mitochondria and displaying allosteric properties, and a non-allosteric, NADP(+)-linked enzyme that is found in both mitochondria and cytoplasm.</rdfs:comment>
<rdfs:comment>The enzyme from some species can also use NAD(+) but much more slowly.</rdfs:comment>
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<rdfs:label>D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH.</rdfs:label>
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<skos:prefLabel>phosphogluconate 2-dehydrogenase</skos:prefLabel>
<skos:altLabel>6-phosphogluconate 2-dehydrogenase</skos:altLabel>
<skos:altLabel>6-phosphogluconic dehydrogenase</skos:altLabel>
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<rdfs:label>6-phospho-D-gluconate + NADP(+) = 6-phospho-2-dehydro-D-gluconate + H(+) + NADPH.</rdfs:label>
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<rdfs:label>6-phospho-D-gluconate + NAD(+) = 6-phospho-2-dehydro-D-gluconate + H(+) + NADH.</rdfs:label>
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<skos:prefLabel>phosphogluconate dehydrogenase (NADP(+)-dependent, decarboxylating)</skos:prefLabel>
<skos:altLabel>6PGD</skos:altLabel>
<skos:altLabel>6-phosphogluconic carboxylase</skos:altLabel>
<skos:altLabel>6-phosphogluconic dehydrogenase</skos:altLabel>
<skos:altLabel>phosphogluconic acid dehydrogenase</skos:altLabel>
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<rdfs:comment>The enzyme participates in the oxidative branch of the pentose phosphate pathway, whose main purpose is to produce NADPH and pentose for biosynthetic reactions.</rdfs:comment>
<rdfs:comment>Highly specific for NADP(+).</rdfs:comment>
<rdfs:comment>Cf. EC 1.1.1.343.</rdfs:comment>
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<rdfs:label>6-phospho-D-gluconate + NADP(+) = CO2 + D-ribulose 5-phosphate + NADPH.</rdfs:label>
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<skos:prefLabel>L-gulonate 3-dehydrogenase</skos:prefLabel>
<skos:altLabel>L-3-aldonate dehydrogenase</skos:altLabel>
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<rdfs:comment>Also oxidizes other L-3-hydroxyacids.</rdfs:comment>
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<rdfs:label>L-gulonate + NAD(+) = 3-dehydro-L-gulonate + H(+) + NADH.</rdfs:label>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>L-arabinose 1-dehydrogenase</skos:prefLabel>
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<rdfs:label>alpha-L-arabinopyanose + NAD(+) = H(+) + L-arabinono-1,4-lactone + NADH.</rdfs:label>
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<skos:prefLabel>glucose 1-dehydrogenase [NAD(P)(+)]</skos:prefLabel>
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<rdfs:comment>This enzyme has similar activity with either NAD(+) or NADP(+).</rdfs:comment>
<rdfs:comment>Cf. EC 1.1.1.118 and EC 1.1.1.119.</rdfs:comment>
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<rdfs:label>D-glucose + NADP(+) = D-glucono-1,5-lactone + H(+) + NADPH.</rdfs:label>
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<skos:prefLabel>D-galactose 1-dehydrogenase</skos:prefLabel>
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<rdfs:comment>This enzyme is part of the De Ley-Doudoroff pathway, which is used by some bacteria during growth on D-galactose.</rdfs:comment>
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<rdfs:label>D-galactose + NAD(+) = D-galactono-1,4-lactone + H(+) + NADH.</rdfs:label>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>glucose-6-phosphate dehydrogenase (NADP(+))</skos:prefLabel>
<skos:altLabel>G6PD</skos:altLabel>
<skos:altLabel>G6PDH</skos:altLabel>
<skos:altLabel>glucose-6-phosphate 1-dehydrogenase</skos:altLabel>
<skos:altLabel>glucose-6-phosphate dehydrogenase</skos:altLabel>
<skos:altLabel>GPD</skos:altLabel>
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<rdfs:comment>The enzyme catalyzes a step of the pentose phosphate pathway.</rdfs:comment>
<rdfs:comment>The enzyme is specific for NADP(+), cf. EC 1.1.1.363 and EC 1.1.1.388.</rdfs:comment>
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<rdfs:label>D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH.</rdfs:label>
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<skos:prefLabel>3alpha-hydroxysteroid 3-dehydrogenase (Si-specific)</skos:prefLabel>
<skos:altLabel>3alpha-HSD</skos:altLabel>
<skos:altLabel>3alpha-hydroxysteroid 3-dehydrogenase (B-specific)</skos:altLabel>
<skos:altLabel>3alpha-hydroxysteroid dehydrogenase (B-specific)</skos:altLabel>
<skos:altLabel>hydroxyprostaglandin dehydrogenase</skos:altLabel>
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<rdfs:comment>The enzyme acts on androsterone and other 3alpha-hydroxysteroids and on 9-, 11- and 15-hydroxyprostaglandin.</rdfs:comment>
<rdfs:comment>Si-specific with respect to NAD(+) or NADP(+) (cf. EC 1.1.1.213).</rdfs:comment>
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<citation rdf:resource="http://purl.uniprot.org/citations/13405910"/>
<citation rdf:resource="http://purl.uniprot.org/citations/14406805"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.50#SIP0C20651CC5E7FC65">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>a 3alpha-hydroxysteroid + NAD(+) = a 3-oxosteroid + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.50#SIPB73B2D324E3434D2">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>a 3alpha-hydroxysteroid + NADP(+) = a 3-oxosteroid + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/3479982">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/13295221">
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/13405910">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/13405910"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/14406805">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/14406805"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/14406805"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.51">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>3(or 17)beta-hydroxysteroid dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.51#SIPCF192CDD1DB5201F"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.51#SIP8197146C6F54D1C0"/>
<rdfs:comment>Also acts on other 3beta- or 17beta-hydroxysteroids (cf. EC 1.1.1.209).</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/193845"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.51#SIPCF192CDD1DB5201F">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>NAD(+) + testosterone = androst-4-ene-3,17-dione + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.51#SIP8197146C6F54D1C0">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>NADP(+) + testosterone = androst-4-ene-3,17-dione + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/193845">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/193845"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/193845"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.52">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>3alpha-hydroxycholanate dehydrogenase (NAD(+))</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.52#SIP01FF5788BA04E368"/>
<rdfs:comment>Also acts on other 3alpha-hydroxysteroids with an acidic side-chain.</rdfs:comment>
<rdfs:comment>Cf. EC 1.1.1.392.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/14377608"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.52#SIP01FF5788BA04E368">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>lithocholate + NAD(+) = 3-oxo-5beta-cholan-24-oate + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/14377608">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/14377608"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/14377608"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.53">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>3alpha(or 20beta)-hydroxysteroid dehydrogenase</skos:prefLabel>
<skos:altLabel>(R)-20-hydroxysteroid dehydrogenase</skos:altLabel>
<skos:altLabel>cortisone reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.53#SIP8DB0E7051278A243"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.53#SIPE5D01D78B2971E21"/>
<rdfs:comment>The 3alpha-hydroxy group or 20beta-hydroxy group of pregnane and androstane steroids can act as donor.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/718844"/>
<citation rdf:resource="http://purl.uniprot.org/citations/6928375"/>
<citation rdf:resource="http://purl.uniprot.org/citations/6936053"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.53#SIP8DB0E7051278A243">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>androstan-3alpha,17beta-diol + NAD(+) = 17beta-hydroxyandrostanone + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.53#SIPE5D01D78B2971E21">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>5alpha-androstane-3alpha,17beta-diol + NAD(+) = 17beta-hydroxy-5alpha-androstan-3-one + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/718844">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/6928375">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/6928375"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/6928375"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/6936053">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/6936053"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/6936053"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.54">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>allyl-alcohol dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.54#SIP80CAC094412755AE"/>
<rdfs:comment>Also acts on saturated primary alcohols.</rdfs:comment>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.54#SIP80CAC094412755AE">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>allyl alcohol + NADP(+) = acrolein + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.55">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>lactaldehyde reductase (NADPH)</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.55#SIP22C8BD49427EA86E"/>
<rdfs:comment>May be identical with EC 1.1.1.2.</rdfs:comment>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.55#SIP22C8BD49427EA86E">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>NADP(+) + propane-1,2-diol = (S)-lactaldehyde + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.56">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>ribitol 2-dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.56#SIP70C6F7D12531D406"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.56#SIP70C6F7D12531D406">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>NAD(+) + ribitol = D-ribulose + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.57">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>fructuronate reductase</skos:prefLabel>
<skos:altLabel>D-mannonate dehydrogenase</skos:altLabel>
<skos:altLabel>D-mannonate oxidoreductase</skos:altLabel>
<skos:altLabel>mannonic dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.57#SIPF0C280BE1F5E5AB2"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.57#SIP6DD307CE66CE32E2"/>
<rdfs:comment>Also reduces D-tagaturonate.</rdfs:comment>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.57#SIPF0C280BE1F5E5AB2">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-mannonate + NAD(+) = H(+) + keto-D-fructuronate + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.57#SIP6DD307CE66CE32E2">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-mannonate + NAD(+) = H(+) + keto-D-tagaturonate + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.58">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>tagaturonate reductase</skos:prefLabel>
<skos:altLabel>altronate dehydrogenase</skos:altLabel>
<skos:altLabel>altronate oxidoreductase</skos:altLabel>
<skos:altLabel>altronic oxidoreductase</skos:altLabel>
<skos:altLabel>Tagaturonate dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.58#SIPF4A45678F2AA42A5"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.58#SIPF4A45678F2AA42A5">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-altronate + NAD(+) = H(+) + keto-D-tagaturonate + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.59">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>3-hydroxypropionate dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.59#SIP4CE8D53F7353E363"/>
<citation rdf:resource="http://purl.uniprot.org/citations/13672942"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.59#SIP4CE8D53F7353E363">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>3-hydroxypropanoate + NAD(+) = 3-oxopropanoate + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/13672942">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/13672942"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/13672942"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.60">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>2-hydroxy-3-oxopropionate reductase</skos:prefLabel>
<skos:altLabel>tartronate semialdehyde reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.60#SIPFD70AEBF3A114703"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.60#SIP50B75E3A2639A8B4"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.60#SIPFD70AEBF3A114703">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(R)-glycerate + NADP(+) = 2-hydroxy-3-oxopropanoate + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.60#SIP50B75E3A2639A8B4">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(R)-glycerate + NAD(+) = 2-hydroxy-3-oxopropanoate + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.61">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>4-hydroxybutyrate dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.61#SIPE65068D2308A8DC8"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.61#SIPE65068D2308A8DC8">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>4-hydroxybutanoate + NAD(+) = H(+) + NADH + succinate semialdehyde.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.62">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>17beta-estradiol 17-dehydrogenase</skos:prefLabel>
<skos:altLabel>17beta-estradiol dehydrogenase</skos:altLabel>
<skos:altLabel>17beta-HSD</skos:altLabel>
<skos:altLabel>17beta-hydroxysteroid dehydrogenase</skos:altLabel>
<skos:altLabel>20alpha-hydroxysteroid dehydrogenase</skos:altLabel>
<skos:altLabel>estrogen 17-oxidoreductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.62#SIPEFEFA3EF10A32DB8"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.62#SIP95CE71F7461A9B6F"/>
<rdfs:comment>The enzyme oxidizes or reduces the hydroxy/keto group on C17 of estrogens and androgens in mammals and regulates the biological potency of these steroids.</rdfs:comment>
<rdfs:comment>The mammalian enzyme is bifunctional and also catalyzes EC 1.1.1.270.</rdfs:comment>
<rdfs:comment>The enzyme also acts on (S)-20-hydroxypregn-4-en-3-one and related compounds, oxidizing the (S)-20-group, but unlike EC 1.1.1.149, it is Si-specific with respect to NAD(P)(+).</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/4314937"/>
<citation rdf:resource="http://purl.uniprot.org/citations/12829805"/>
<citation rdf:resource="http://purl.uniprot.org/citations/14413943"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.62#SIPEFEFA3EF10A32DB8">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>17beta-estradiol + NAD(+) = estrone + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.62#SIP95CE71F7461A9B6F">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>17beta-estradiol + NADP(+) = estrone + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/4314937">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/12829805">
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/14413943">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/14413943"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/14413943"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.63">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<obsolete rdf:datatype="http://www.w3.org/2001/XMLSchema#boolean">true</obsolete>
<replacedBy rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.239"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.64">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>testosterone 17beta-dehydrogenase (NADP(+))</skos:prefLabel>
<skos:altLabel>17-ketoreductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.64#SIP8197146C6F54D1C0"/>
<rdfs:comment>Also oxidizes 3-hydroxyhexobarbital to 3-oxohexobarbital.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/13696735"/>
<citation rdf:resource="http://purl.uniprot.org/citations/13781425"/>
<citation rdf:resource="http://purl.uniprot.org/citations/15436478"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.64#SIP8197146C6F54D1C0">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>NADP(+) + testosterone = androst-4-ene-3,17-dione + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/13696735">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/13696735"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/citations/13781425">
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<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/13781425"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/citations/15436478">
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<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/15436478"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/15436478"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.65">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>pyridoxine 4-dehydrogenase</skos:prefLabel>
<skos:altLabel>PL reductase</skos:altLabel>
<skos:altLabel>pyridoxal reductase</skos:altLabel>
<skos:altLabel>pyridoxine dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.65#SIPE8471F81FF1BAEDC"/>
<rdfs:comment>Also oxidizes pyridoxine phosphate.</rdfs:comment>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.65#SIPE8471F81FF1BAEDC">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>NADP(+) + pyridoxine = H(+) + NADPH + pyridoxal.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.66">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>omega-hydroxydecanoate dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.66#SIPD77CF7E8E31AF490"/>
<rdfs:comment>Also acts, more slowly, on 9-hydroxynonanoate and 11-hydroxyundecanoate.</rdfs:comment>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.66#SIPD77CF7E8E31AF490">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>10-hydroxydecanoate + NAD(+) = 10-oxodecanoate + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.67">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>mannitol 2-dehydrogenase</skos:prefLabel>
<skos:altLabel>mannitol dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.67#SIP14C692C4E8D7034D"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.67#SIP14C692C4E8D7034D">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-mannitol + NAD(+) = D-fructose + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.68">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<obsolete rdf:datatype="http://www.w3.org/2001/XMLSchema#boolean">true</obsolete>
<replacedBy rdf:resource="http://purl.uniprot.org/enzyme/1.5.1.20"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.69">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>gluconate 5-dehydrogenase</skos:prefLabel>
<skos:altLabel>5-keto-D-gluconate 5-reductase</skos:altLabel>
<skos:altLabel>5-ketogluconate 5-reductase</skos:altLabel>
<skos:altLabel>5-ketogluconate reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.69#SIP108E818F61EC71B5"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.69#SIPD366298693B607B3"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.69#SIP108E818F61EC71B5">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-gluconate + NADP(+) = 5-dehydro-D-gluconate + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.69#SIPD366298693B607B3">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-gluconate + NAD(+) = 5-dehydro-D-gluconate + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.70">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<obsolete rdf:datatype="http://www.w3.org/2001/XMLSchema#boolean">true</obsolete>
<replacedBy rdf:resource="http://purl.uniprot.org/enzyme/1.2.1.3"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.71">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>alcohol dehydrogenase [NAD(P)(+)]</skos:prefLabel>
<skos:altLabel>retinal reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.71#SIP8826B9F272890D4B"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.71#SIP85407D6214AA0FCB"/>
<rdfs:comment>Reduces aliphatic aldehydes of chain length from C2 to C14, with greatest activity on C4, C6 and C8 aldehydes.</rdfs:comment>
<rdfs:comment>Also reduces retinal to retinol.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/4300551"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.71#SIP8826B9F272890D4B">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.71#SIP85407D6214AA0FCB">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>a primary alcohol + NADP(+) = an aldehyde + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/4300551">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/4300551"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.72">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>glycerol dehydrogenase (NADP(+))</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.72#SIP33BFD81643982BE9"/>
<citation rdf:resource="http://purl.uniprot.org/citations/4400494"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.72#SIP33BFD81643982BE9">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>glycerol + NADP(+) = D-glyceraldehyde + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/4400494">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/4400494"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/4400494"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.73">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>octanol dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.73#SIPC5B7720EF0F0699B"/>
<rdfs:comment>Acts, less rapidly, on other long-chain alcohols.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/4308448"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.73#SIPC5B7720EF0F0699B">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>NAD(+) + octan-1-ol = H(+) + NADH + octanal.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/4308448">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/4308448"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/4308448"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.74">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<obsolete rdf:datatype="http://www.w3.org/2001/XMLSchema#boolean">true</obsolete>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.75">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>(R)-aminopropanol dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.75#SIP2E86E9730BB773A1"/>
<citation rdf:resource="http://purl.uniprot.org/citations/4385233"/>
<citation rdf:resource="http://purl.uniprot.org/citations/5329339"/>
<citation rdf:resource="http://purl.uniprot.org/citations/5340733"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.75#SIP2E86E9730BB773A1">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(R)-1-aminopropan-2-ol + NAD(+) = aminoacetone + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/4385233">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/4385233"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/4385233"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/5329339">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/5329339"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/5329339"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/5340733">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/5340733"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/5340733"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.76">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>(S,S)-butanediol dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.76#SIP13BC1D556315284D"/>
<rdfs:comment>This enzyme catalyzes the reversible reduction of (S)-acetoin to (S,S)-butane-2,3-diol.</rdfs:comment>
<rdfs:comment>It can also catalyze the irreversible reduction of diacetyl to (S)-acetoin.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/2040298"/>
<citation rdf:resource="http://purl.uniprot.org/citations/11577733"/>
<citation rdf:resource="http://purl.uniprot.org/citations/13837186"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.76#SIP13BC1D556315284D">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(S,S)-butane-2,3-diol + NAD(+) = (S)-acetoin + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/2040298">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/2040298"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/2040298"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/11577733">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/11577733"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/13837186">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/13837186"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/13837186"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.77">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>lactaldehyde reductase</skos:prefLabel>
<skos:altLabel>propanediol oxidoreductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.77#SIP2A81AFF0F0735C9F"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.77#SIPBCCE65E4AF1BA761"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.77#SIP2A81AFF0F0735C9F">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(R)-propane-1,2-diol + NAD(+) = (R)-lactaldehyde + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.77#SIPBCCE65E4AF1BA761">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(S)-propane-1,2-diol + NAD(+) = (S)-lactaldehyde + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.78">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>methylglyoxal reductase (NADH)</skos:prefLabel>
<skos:altLabel>D-lactaldehyde dehydrogenase</skos:altLabel>
<skos:altLabel>methylglyoxal reductase</skos:altLabel>
<skos:altLabel>methylglyoxal reductase (NADH-dependent)</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.78#SIP55196B0AB897502B"/>
<rdfs:comment>This mammalian enzyme differs from the yeast enzyme, EC 1.1.1.283, by its coenzyme requirement, reaction direction, and enantiomeric preference.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/6386056"/>
<citation rdf:resource="http://purl.uniprot.org/citations/14323585"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.78#SIP55196B0AB897502B">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(R)-lactaldehyde + NAD(+) = H(+) + methylglyoxal + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/6386056">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/6386056"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/6386056"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/14323585">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/14323585"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/14323585"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.79">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>glyoxylate reductase (NADP(+))</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.79#SIP921B5C69E2CAA022"/>
<rdfs:comment>Also reduces hydroxypyruvate to glycerate.</rdfs:comment>
<rdfs:comment>Has some affinity for NAD(+).</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/3548703"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.79#SIP921B5C69E2CAA022">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>glycolate + NADP(+) = glyoxylate + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/3548703">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/3548703"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/3548703"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.80">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>isopropanol dehydrogenase (NADP(+))</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.80#SIP9DD9C804739442C9"/>
<rdfs:comment>Also acts on other short-chain secondary alcohols and, slowly, on primary alcohols.</rdfs:comment>
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<rdfs:label>NADP(+) + propan-2-ol = acetone + H(+) + NADPH.</rdfs:label>
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<skos:prefLabel>hydroxypyruvate reductase</skos:prefLabel>
<skos:altLabel>D-glycerate dehydrogenase</skos:altLabel>
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<rdfs:label>(R)-glycerate + NAD(+) = 3-hydroxypyruvate + H(+) + NADH.</rdfs:label>
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<rdfs:label>(R)-glycerate + NADP(+) = 3-hydroxypyruvate + H(+) + NADPH.</rdfs:label>
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<skos:prefLabel>malate dehydrogenase (NADP(+))</skos:prefLabel>
<skos:altLabel>NADP-linked malate dehydrogenase</skos:altLabel>
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<rdfs:comment>Activated by light.</rdfs:comment>
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<rdfs:label>(S)-malate + NADP(+) = H(+) + NADPH + oxaloacetate.</rdfs:label>
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<skos:prefLabel>D-malate dehydrogenase (decarboxylating)</skos:prefLabel>
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<rdfs:label>(R)-malate + NAD(+) = CO2 + NADH + pyruvate.</rdfs:label>
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<skos:prefLabel>dimethylmalate dehydrogenase</skos:prefLabel>
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<rdfs:comment>Also acts on (R)-malate.</rdfs:comment>
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<rdfs:label>(R)-3,3-dimethylmalate + NAD(+) = 3-methyl-2-oxobutanoate + CO2 + NADH.</rdfs:label>
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<skos:prefLabel>3-isopropylmalate dehydrogenase</skos:prefLabel>
<skos:altLabel>beta-IPM dehydrogenase</skos:altLabel>
<skos:altLabel>beta-isopropylmalate dehydrogenase</skos:altLabel>
<skos:altLabel>IMDH</skos:altLabel>
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<rdfs:label>(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO2 + NADH.</rdfs:label>
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<skos:prefLabel>ketol-acid reductoisomerase (NADP(+))</skos:prefLabel>
<skos:altLabel>acetohydroxy acid isomeroreductase</skos:altLabel>
<skos:altLabel>alpha-keto-beta-hydroxylacyl reductoisomerase</skos:altLabel>
<skos:altLabel>dihydroxyisovalerate dehydrogenase (isomerizing)</skos:altLabel>
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<rdfs:comment>The enzyme, found in many bacteria and archaea, is specific for NADPH (cf. EC 1.1.1.382 and EC 1.1.1.383).</rdfs:comment>
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<rdfs:label>(2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-acetolactate + H(+) + NADPH.</rdfs:label>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.86#SIP107E4B2D53FCD9B0">
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<rdfs:label>(2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)-2-ethyl-2-hydroxy-3-oxobutanoate + H(+) + NADPH.</rdfs:label>
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<skos:prefLabel>homoisocitrate dehydrogenase</skos:prefLabel>
<skos:altLabel>(-)-1-hydroxy-1,2,4-butanetricarboxylate:NAD(+) oxidoreductase (decarboxylating)</skos:altLabel>
<skos:altLabel>2-hydroxy-3-carboxyadipate dehydrogenase</skos:altLabel>
<skos:altLabel>3-carboxy-2-hydroxyadipate:NAD(+) oxidoreductase (decarboxylating)</skos:altLabel>
<skos:altLabel>3-carboxy-2-hydroxyadipate dehydrogenase</skos:altLabel>
<skos:altLabel>homoisocitric dehydrogenase</skos:altLabel>
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<rdfs:comment>Forms part of the lysine biosynthesis pathway in fungi.</rdfs:comment>
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<rdfs:label>(2R,3S)-homoisocitrate + NAD(+) = 2-oxoadipate + CO2 + NADH.</rdfs:label>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>hydroxymethylglutaryl-CoA reductase</skos:prefLabel>
<skos:altLabel>3-hydroxy-3-methylglutaryl coenzyme A reductase</skos:altLabel>
<skos:altLabel>beta-hydroxy-beta-methylglutaryl CoA-reductase</skos:altLabel>
<skos:altLabel>beta-hydroxy-beta-methylglutaryl coenzyme A reductase</skos:altLabel>
<skos:altLabel>HMG-CoA reductase</skos:altLabel>
<skos:altLabel>hydroxymethylglutaryl coenzyme A reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.88#SIP03D126AF46B124D6"/>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(R)-mevalonate + CoA + 2 NAD(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADH.</rdfs:label>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.89">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<obsolete rdf:datatype="http://www.w3.org/2001/XMLSchema#boolean">true</obsolete>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>aryl-alcohol dehydrogenase</skos:prefLabel>
<skos:altLabel>benzyl alcohol dehydrogenase</skos:altLabel>
<skos:altLabel>p-hydroxybenzyl alcohol dehydrogenase</skos:altLabel>
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<rdfs:comment>A group of enzymes with broad specificity toward primary alcohols with an aromatic or cyclohex-1-ene ring, but with low or no activity toward short-chain aliphatic alcohols.</rdfs:comment>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.90#SIP8D6B7BE9637F4CF0">
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<rdfs:label>an aromatic primary alcohol + NAD(+) = an aromatic aldehyde + H(+) + NADH.</rdfs:label>
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<skos:prefLabel>aryl-alcohol dehydrogenase (NADP(+))</skos:prefLabel>
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<rdfs:comment>Also acts on some aliphatic aldehydes, but cinnamaldehyde was the best substrate found.</rdfs:comment>
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<rdfs:label>an aromatic primary alcohol + NADP(+) = an aromatic aldehyde + H(+) + NADPH.</rdfs:label>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>oxaloglycolate reductase (decarboxylating)</skos:prefLabel>
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<rdfs:comment>Also reduces hydroxypyruvate to D-glycerate and glyoxylate to glycolate.</rdfs:comment>
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<rdfs:label>(R)-glycerate + CO2 + NAD(+) = 2-hydroxy-3-oxosuccinate + 2 H(+) + NADH.</rdfs:label>
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<rdfs:label>(R)-glycerate + CO2 + NADP(+) = 2-hydroxy-3-oxosuccinate + 2 H(+) + NADPH.</rdfs:label>
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<skos:prefLabel>tartrate dehydrogenase</skos:prefLabel>
<skos:altLabel>mesotartrate dehydrogenase</skos:altLabel>
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<rdfs:label>NAD(+) + tartrate = 2-hydroxy-3-oxosuccinate + H(+) + NADH.</rdfs:label>
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<rdfs:label>(2R,3S)-tartrate + NAD(+) = 2-hydroxy-3-oxosuccinate + H(+) + NADH.</rdfs:label>
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<rdfs:label>(2R,3R)-tartrate + NAD(+) = 2-hydroxy-3-oxosuccinate + H(+) + NADH.</rdfs:label>
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<skos:prefLabel>glycerol-3-phosphate dehydrogenase [NAD(P)(+)]</skos:prefLabel>
<skos:altLabel>glycerol 3-phosphate dehydrogenase (NAD(P))</skos:altLabel>
<skos:altLabel>glycerol 3-phosphate dehydrogenase (NADP)</skos:altLabel>
<skos:altLabel>glycerol phosphate dehydrogenase (nicotinamide adenine dinucleotide (phosphate))</skos:altLabel>
<skos:altLabel>L-glycerol-3-phosphate:NAD(P) oxidoreductase</skos:altLabel>
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<rdfs:comment>The enzyme from Escherichia coli shows specificity for the B side of NADPH.</rdfs:comment>
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<rdfs:label>NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH.</rdfs:label>
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<rdfs:label>NADP(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADPH.</rdfs:label>
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<skos:prefLabel>phosphoglycerate dehydrogenase</skos:prefLabel>
<skos:altLabel>3-phosphoglycerate dehydrogenase</skos:altLabel>
<skos:altLabel>3-phosphoglyceric acid dehydrogenase</skos:altLabel>
<skos:altLabel>3PHP reductase</skos:altLabel>
<skos:altLabel>alphaKG reductase</skos:altLabel>
<skos:altLabel>alpha-phosphoglycerate dehydrogenase</skos:altLabel>
<skos:altLabel>D-3-phosphoglycerate dehydrogenase</skos:altLabel>
<skos:altLabel>glycerate-1,3-phosphate dehydrogenase</skos:altLabel>
<skos:altLabel>glycerate 3-phosphate dehydrogenase</skos:altLabel>
<skos:altLabel>PGDH</skos:altLabel>
<skos:altLabel>phosphoglycerate oxidoreductase</skos:altLabel>
<skos:altLabel>phosphoglyceric acid dehydrogenase</skos:altLabel>
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<rdfs:comment>Catalyzes the first committed and rate-limiting step in the phosphoserine pathway of serine biosynthesis.</rdfs:comment>
<rdfs:comment>The reaction occurs predominantly in the direction of reduction.</rdfs:comment>
<rdfs:comment>The enzyme from the bacterium Escherichia coli also catalyzes the activity of EC 1.1.1.399.</rdfs:comment>
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<rdfs:label>(2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+) + NADH.</rdfs:label>
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<skos:prefLabel>diiodophenylpyruvate reductase</skos:prefLabel>
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<rdfs:comment>Substrates contain an aromatic ring with a pyruvate side chain.</rdfs:comment>
<rdfs:comment>The most active substrates are halogenated derivatives.</rdfs:comment>
<rdfs:comment>Compounds with hydroxy or amino groups in the 3 or 5 position are inactive.</rdfs:comment>
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<rdfs:label>3-(3,5-diiodo-4-hydroxyphenyl)lactate + NAD(+) = 3-(3,5-diiodo-4-hydroxyphenyl)pyruvate + H(+) + NADH.</rdfs:label>
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<rdfs:label>(2R)-2-hydroxy-3-(4-hydroxyphenyl)propanoate + NAD(+) = 3-(4-hydroxyphenyl)pyruvate + H(+) + NADH.</rdfs:label>
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<dcterms:identifier>doi:10.1016/s0021-9258(18)96779-7</dcterms:identifier>
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<skos:prefLabel>3-hydroxybenzyl-alcohol dehydrogenase</skos:prefLabel>
<skos:altLabel>m-hydroxybenzyl alcohol dehydrogenase</skos:altLabel>
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<rdfs:label>3-hydroxybenzyl alcohol + NADP(+) = 3-hydroxybenzaldehyde + H(+) + NADPH.</rdfs:label>
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<skos:prefLabel>(R)-2-hydroxy-fatty-acid dehydrogenase</skos:prefLabel>
<skos:altLabel>D-2-hydroxy fatty acid dehydrogenase</skos:altLabel>
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<rdfs:label>(R)-2-hydroxyoctadecanoate + NAD(+) = 2-oxooctadecanoate + H(+) + NADH.</rdfs:label>
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<skos:prefLabel>(S)-2-hydroxy-fatty-acid dehydrogenase</skos:prefLabel>
<skos:altLabel>L-2-hydroxy fatty acid dehydrogenase</skos:altLabel>
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<rdfs:label>(S)-2-hydroxyoctadecanoate + NAD(+) = 2-oxooctadecanoate + H(+) + NADH.</rdfs:label>
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<skos:prefLabel>3-oxoacyl-[acyl-carrier-protein] reductase</skos:prefLabel>
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<rdfs:comment>Exhibits a marked preference for [acyl-carrier-protein] derivatives over CoA derivatives as substrates.</rdfs:comment>
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<rdfs:label>a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) + NADPH.</rdfs:label>
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<skos:prefLabel>acylglycerone-phosphate reductase</skos:prefLabel>
<skos:altLabel>palmitoyldihydroxyacetone-phosphate reductase</skos:altLabel>
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<rdfs:comment>Also acts on alkylglycerone 3-phosphate and alkylglycerol 3-phosphate.</rdfs:comment>
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<rdfs:label>1-hexadecanoyl-sn-glycero-3-phosphate + NADP(+) = 1-hexadecanoylglycerone 3-phosphate + H(+) + NADPH.</rdfs:label>
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<rdfs:label>1-O-alkylglycerone 3-phosphate + H(+) + NADPH = 1-O-alkyl-sn-glycero-3-phosphate + NADP(+).</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.102">
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<skos:prefLabel>3-dehydrosphinganine reductase</skos:prefLabel>
<skos:altLabel>3-ketosphinganine reductase</skos:altLabel>
<skos:altLabel>3-oxosphinganine:NADPH oxidoreductase</skos:altLabel>
<skos:altLabel>3-oxosphinganine reductase</skos:altLabel>
<skos:altLabel>D-3-dehydrosphinganine reductase</skos:altLabel>
<skos:altLabel>D-3-oxosphinganine:B-NADPH oxidoreductase</skos:altLabel>
<skos:altLabel>D-3-oxosphinganine reductase</skos:altLabel>
<skos:altLabel>DSR</skos:altLabel>
<skos:altLabel>KTS reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.102#SIP9731D71EACFEE1DA"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.102#SIP9731D71EACFEE1DA">
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<rdfs:label>NADP(+) + sphinganine = 3-oxosphinganine + H(+) + NADPH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.103">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>L-threonine 3-dehydrogenase</skos:prefLabel>
<skos:altLabel>TDH</skos:altLabel>
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<rdfs:comment>Acts in concert with EC 2.3.1.29 in the degradation of threonine to glycine.</rdfs:comment>
<rdfs:comment>This threonine-degradation pathway is common to prokaryotic and eukaryotic cells and the two enzymes involved form a complex.</rdfs:comment>
<rdfs:comment>In aqueous solution, the product L-2-amino-3-oxobutanoate can spontaneously decarboxylate to form aminoacetone.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/7548"/>
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<rdfs:label>L-threonine + NAD(+) = (2S)-2-amino-3-oxobutanoate + H(+) + NADH.</rdfs:label>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.104">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>4-oxoproline reductase</skos:prefLabel>
<skos:altLabel>cis-hydroxy-L-proline oxidase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.104#SIP410B331A600740CD"/>
<rdfs:comment>The enzyme, isolated from animals, is specific for 4-oxo-L-proline and cis-4-hydroxy-L-proline.</rdfs:comment>
<rdfs:comment>It has no activity with trans-4-hydroxy-L-proline.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/13914427"/>
<citation rdf:resource="http://purl.uniprot.org/citations/35150746"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.104#SIP410B331A600740CD">
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<rdfs:label>cis-4-hydroxy-L-proline + NAD(+) = 4-oxo-L-proline + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<dcterms:identifier>doi:10.1016/j.jbc.2022.101708</dcterms:identifier>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.105">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>all-trans-retinol dehydrogenase (NAD(+))</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.105#SIP395445F2445E9179"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.105#SIP725E0E748DA989CC"/>
<rdfs:comment>The enzyme recognizes all-trans-retinol and all-trans-retinal as substrates and exhibits a strong preference for NAD(+)/NADH as cofactors.</rdfs:comment>
<rdfs:comment>Recognizes the substrate both in free form and when bound to cellular-retinol-binding-protein (CRBP1), but has higher affinity for the bound form.</rdfs:comment>
<rdfs:comment>No activity with 11-cis-retinol or 11-cis-retinal (cf. EC 1.1.1.315).</rdfs:comment>
<rdfs:comment>Also active with 3alpha-hydroxysteroids.</rdfs:comment>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.105#SIP395445F2445E9179">
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<rdfs:label>all-trans-retinol--[retinol-binding protein] + NAD(+) = all-trans-retinal--[retinol-binding protein] + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdfs:label>all-trans-retinol + NAD(+) = all-trans-retinal + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.106">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>pantoate 4-dehydrogenase</skos:prefLabel>
<skos:altLabel>Panthothenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.106#SIP4A47720CDC72325F"/>
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<rdfs:label>(R)-pantoate + NAD(+) = (R)-4-dehydropantoate + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.107">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>pyridoxal 4-dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.107#SIP68D3030A5D73B0B5"/>
<rdfs:comment>The enzyme acts on the hemiacetal form of the substrate.</rdfs:comment>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.107#SIP68D3030A5D73B0B5">
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<rdfs:label>NAD(+) + pyridoxal = 4-pyridoxolactone + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.108">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>carnitine 3-dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.108#SIP4A84692E625B3215"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.108#SIP4A84692E625B3215">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>carnitine + NAD(+) = 3-dehydrocarnitine + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.109">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<obsolete rdf:datatype="http://www.w3.org/2001/XMLSchema#boolean">true</obsolete>
<replacedBy rdf:resource="http://purl.uniprot.org/enzyme/1.3.1.28"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.110">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<replaces rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.222"/>
<skos:prefLabel>aromatic 2-oxoacid reductase</skos:prefLabel>
<skos:altLabel>(R)-4-hydroxyphenyllactate dehydrogenase</skos:altLabel>
<skos:altLabel>(R)-aromatic lactate dehydrogenase</skos:altLabel>
<skos:altLabel>indole-3-lactate dehydrogenase</skos:altLabel>
<skos:altLabel>indolelactate dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.110#SIP2C760EA5F427C331"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.110#SIP5590D5860E490B6F"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.110#SIP9E390E9CA8705C97"/>
<rdfs:comment>The enzymes from anaerobic bacteria such as Clostridium sporogenes participate in the fermentation pathways of L-phenylalanine, L-tyrosine and L-tryptophan.</rdfs:comment>
<rdfs:comment>The enzyme from the yeast Candida maltosa has similar activity, but, unlike the bacterial enzyme, requires Mn(2+) and can also use NADPH with lower activity.</rdfs:comment>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(R)-3-phenyllactate + NAD(+) = 3-phenylpyruvate + H(+) + NADH.</rdfs:label>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.110#SIP5590D5860E490B6F">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(2R)-2-hydroxy-3-(4-hydroxyphenyl)propanoate + NAD(+) = 3-(4-hydroxyphenyl)pyruvate + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>3-(indol-3-yl)lactate + NAD(+) = H(+) + indole-3-pyruvate + NADH.</rdfs:label>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.111">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>3-(imidazol-5-yl)lactate dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.111#SIPA030586FDBC9ACE5"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.111#SIPD99F65613D48B5EA"/>
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<rdfs:label>(S)-3-(imidazol-5-yl)lactate + NAD(+) = 3-(imidazol-5-yl)pyruvate + H(+) + NADH.</rdfs:label>
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<rdfs:label>(S)-3-(imidazol-5-yl)lactate + NADP(+) = 3-(imidazol-5-yl)pyruvate + H(+) + NADPH.</rdfs:label>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.112">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>indanol dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.112#SIPC260A58AC9E9AEA1"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.112#SIP745DD9DE7931757A"/>
<rdfs:comment>3(20)alpha-hydroxysteroids are also oxidized, more slowly.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/2559080"/>
<citation rdf:resource="http://purl.uniprot.org/citations/4397102"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.112#SIPC260A58AC9E9AEA1">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(S)-indan-1-ol + NAD(+) = H(+) + indan-1-one + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.112#SIP745DD9DE7931757A">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(S)-indan-1-ol + NADP(+) = H(+) + indan-1-one + NADPH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.113">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>L-xylose 1-dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.113#SIP3903B0FA7CB945B8"/>
<rdfs:comment>Also oxidizes D-arabinose and D-lyxose.</rdfs:comment>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.113#SIP3903B0FA7CB945B8">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>L-xylose + NADP(+) = H(+) + L-xylono-1,4-lactone + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.114">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>apiose 1-reductase</skos:prefLabel>
<skos:altLabel>D-apiitol reductase</skos:altLabel>
<skos:altLabel>D-apiose reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.114#SIP9195AD50ACE43AC6"/>
<citation rdf:resource="http://purl.uniprot.org/citations/4314545"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.114#SIP9195AD50ACE43AC6">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-apiitol + NAD(+) = aldehydo-D-apiose + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/4314545">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/4314545"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.115">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>ribose 1-dehydrogenase (NADP(+))</skos:prefLabel>
<skos:altLabel>NADP-pentose-dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.115#SIP4AD8644F49EF1E58"/>
<rdfs:comment>Also acts, more slowly, on D-xylose and other pentoses.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/4381350"/>
<citation rdf:resource="http://purl.uniprot.org/citations/4393642"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.115#SIP4AD8644F49EF1E58">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-ribose + H2O + NADP(+) = D-ribonate + 2 H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/4381350">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
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<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/4381350"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/4393642">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/4393642"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/4393642"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.116">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>D-arabinose 1-dehydrogenase (NAD(+))</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.116#SIP276DC12FAD5E148A"/>
<citation rdf:resource="http://purl.uniprot.org/citations/4393642"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.116#SIP276DC12FAD5E148A">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-arabinose + NAD(+) = D-arabinono-1,4-lactone + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/4393642">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.117">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>D-arabinose 1-dehydrogenase [NAD(P)(+)]</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.117#SIP5E60F0C9EC055021"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.117#SIP276DC12FAD5E148A"/>
<rdfs:comment>Also acts on L-galactose, 6-deoxy- and 3,6-dideoxy-L-galactose.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/5845847"/>
<citation rdf:resource="http://purl.uniprot.org/citations/5845848"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.117#SIP5E60F0C9EC055021">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-arabinose + NADP(+) = D-arabinono-1,4-lactone + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.117#SIP276DC12FAD5E148A">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-arabinose + NAD(+) = D-arabinono-1,4-lactone + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/5845848"/>
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<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/5845849"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.118">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>glucose 1-dehydrogenase (NAD(+))</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.118#SIP573AF37EBE72B77E"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.118#SIP573AF37EBE72B77E">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-glucose + NAD(+) = D-glucono-1,5-lactone + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.119">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>glucose 1-dehydrogenase (NADP(+))</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.119#SIPA8FD677859758569"/>
<rdfs:comment>Also oxidizes D-mannose, 2-deoxy-D-glucose and 2-amino-2-deoxy-D-mannose.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/4384672"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.119#SIPA8FD677859758569">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-glucose + NADP(+) = D-glucono-1,5-lactone + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/4384672">
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.120">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>galactose 1-dehydrogenase (NADP(+))</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.120#SIP0F4396A50B830C07"/>
<rdfs:comment>Also acts on L-arabinose, 6-deoxy- and 2-deoxy-D-galactose.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/4387016"/>
<citation rdf:resource="http://purl.uniprot.org/citations/5845847"/>
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<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.120#SIP0F4396A50B830C07">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-galactose + NADP(+) = D-galactono-1,5-lactone + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/4387016">
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<rdf:Description rdf:about="http://purl.uniprot.org/citations/5845847">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
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<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/5845847"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/5845848">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
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<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/5845848"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/citations/5845849">
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<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/5845849"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.121">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>aldose 1-dehydrogenase (NAD(+))</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.121#SIP0B0832D01DAC8F7C"/>
<rdfs:comment>Acts on D-glucose, 2-deoxy- and 6-deoxy-D-glucose, D-galactose, 6-deoxy-D-galactose, 2-deoxy-L-arabinose and D-xylose.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/5845847"/>
<citation rdf:resource="http://purl.uniprot.org/citations/5845848"/>
<citation rdf:resource="http://purl.uniprot.org/citations/5845849"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.121#SIP0B0832D01DAC8F7C">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>an aldopyranose + NAD(+) = aldono-1,5-lactone + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/5845847">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/citations/5845848">
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<rdf:Description rdf:about="http://purl.uniprot.org/citations/5845849">
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.122">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>D-threo-aldose 1-dehydrogenase</skos:prefLabel>
<skos:altLabel>(2S,3R)-aldose dehydrogenase</skos:altLabel>
<skos:altLabel>L-fucose dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.122#SIP89A295CB24214662"/>
<rdfs:comment>Acts on L-fucose, D-arabinose and L-xylose.</rdfs:comment>
<rdfs:comment>The animal enzyme was also shown to act on L-arabinose, and the enzyme from Pseudomonas caryophylli on L-glucose.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/40609"/>
<citation rdf:resource="http://purl.uniprot.org/citations/4309152"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.122#SIP89A295CB24214662">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>a D-threo-aldose + NAD(+) = a D-threo-aldono-1,5-lactone + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/40609">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
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<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/40609"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/citations/4309152">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/4309152"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/4309152"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.123">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>sorbose 5-dehydrogenase (NADP(+))</skos:prefLabel>
<skos:altLabel>5-ketofructose reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.123#SIP70228E393171212A"/>
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<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.123#SIP70228E393171212A">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>keto-L-sorbose + NADP(+) = 5-dehydro-D-fructose + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/4392628">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/4392628"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.124">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>fructose 5-dehydrogenase (NADP(+))</skos:prefLabel>
<skos:altLabel>5-ketofructose reductase (NADP(+))</skos:altLabel>
<skos:altLabel>5-ketofructose reductase (NADP+)</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.124#SIP6E80DC5B3652D61B"/>
<citation rdf:resource="http://purl.uniprot.org/citations/4379259"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.124#SIP6E80DC5B3652D61B">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-fructose + NADP(+) = 5-dehydro-D-fructose + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/4379259">
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.125">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>2-deoxy-D-gluconate 3-dehydrogenase</skos:prefLabel>
<skos:altLabel>2-deoxygluconate dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.125#SIPD5DABCDA0DAC8D28"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.125#SIPD5DABCDA0DAC8D28">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>2-deoxy-D-gluconate + NAD(+) = 3-dehydro-2-deoxy-D-gluconate + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.126">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>2-dehydro-3-deoxy-D-gluconate 6-dehydrogenase</skos:prefLabel>
<skos:altLabel>2-keto-3-deoxy-D-gluconate dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.126#SIPD1532385F35A4D31"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.126#SIPD1532385F35A4D31">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>2-dehydro-3-deoxy-D-gluconate + NADP(+) = (4S,5S)-4,5-dihydroxy-2,6-dioxohexanoate + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.127">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase</skos:prefLabel>
<skos:altLabel>2-keto-3-deoxy-D-gluconate dehydrogenase</skos:altLabel>
<skos:altLabel>2-keto-3-deoxygluconate dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.127#SIPE81284D93F317976"/>
<rdfs:comment>The enzyme from Pseudomonas acts equally well on NAD(+) or NADP(+), while those from Erwinia chrysanthemi and Escherichia coli are more specific for NAD(+).</rdfs:comment>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.127#SIPE81284D93F317976">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>2-dehydro-3-deoxy-D-gluconate + NAD(+) = 3-deoxy-D-glycero-2,5-hexodiulosonate + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.128">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<obsolete rdf:datatype="http://www.w3.org/2001/XMLSchema#boolean">true</obsolete>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.129">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>L-threonate 3-dehydrogenase</skos:prefLabel>
<skos:altLabel>L-threonic acid dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.129#SIP985E3669899B4746"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.129#SIP985E3669899B4746">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>L-threonate + NAD(+) = 3-dehydro-D-erythronate + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.130">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>3-dehydro-L-gulonate 2-dehydrogenase</skos:prefLabel>
<skos:altLabel>2,3-diketo-L-gulonate reductase</skos:altLabel>
<skos:altLabel>3-keto-L-gulonate dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.130#SIPFF6F158A08B152D3"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.130#SIPA411146D99088D9D"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.130#SIPFF6F158A08B152D3">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>3-dehydro-L-gulonate + NAD(+) = 2,3-dioxo-L-gulonate + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.130#SIPA411146D99088D9D">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>3-dehydro-L-gulonate + NADP(+) = 2,3-dioxo-L-gulonate + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.131">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<replaces rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.180"/>
<replaces rdf:resource="http://purl.uniprot.org/enzyme/1.2.1.34"/>
<skos:prefLabel>mannuronate reductase</skos:prefLabel>
<skos:altLabel>mannonate dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.131#SIPE83D8B58D95941BC"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.131#SIPEAA1E10933A07DA7"/>
<citation rdf:resource="http://purl.uniprot.org/citations/4388117"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.131#SIPE83D8B58D95941BC">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-mannonate + NAD(+) = D-mannuronate + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.131#SIPEAA1E10933A07DA7">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-mannonate + NADP(+) = D-mannuronate + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/4388117">
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.132">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>GDP-mannose 6-dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.132#SIPCC7BE5F0B0321281"/>
<rdfs:comment>Also uses the corresponding deoxynucleoside diphosphate derivative as a substrate.</rdfs:comment>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.132#SIPCC7BE5F0B0321281">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>GDP-alpha-D-mannose + H2O + 2 NAD(+) = GDP-alpha-D-mannuronate + 3 H(+) + 2 NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.133">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>dTDP-4-dehydrorhamnose reductase</skos:prefLabel>
<skos:altLabel>dTDP-4-keto-L-rhamnose reductase</skos:altLabel>
<skos:altLabel>dTDP-6-deoxy-L-mannose dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.133#SIP2BDF36C49BB7A934"/>
<rdfs:comment>In the reverse direction, reduction on the 4-position of the hexose moiety takes place only while the substrate is bound to another enzyme that catalyzes epimerization at C-3 and C-5; the complex has been referred to as dTDP-L-rhamnose synthase.</rdfs:comment>
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<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.133#SIP2BDF36C49BB7A934">
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<rdfs:label>dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.134">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>dTDP-6-deoxy-L-talose 4-dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.134#SIP79CD9B5E40BD2D29"/>
<rdfs:comment>Oxidation on the 4-position of the hexose moiety takes place only while the substrate is bound to another enzyme that catalyzes epimerization at C-3 and C-5.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/4199258"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.134#SIP79CD9B5E40BD2D29">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>dTDP-6-deoxy-beta-L-talose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH.</rdfs:label>
</rdf:Description>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.135">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>GDP-6-deoxy-D-talose 4-dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.135#SIP745EEB7F5739C476"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.135#SIPBB803B5B08738979"/>
<citation rdf:resource="http://purl.uniprot.org/citations/14209931"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.135#SIP745EEB7F5739C476">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>GDP-6-deoxy-alpha-D-talose + NADP(+) = GDP-4-dehydro-alpha-D-rhamnose + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.135#SIPBB803B5B08738979">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>GDP-6-deoxy-alpha-D-talose + NAD(+) = GDP-4-dehydro-alpha-D-rhamnose + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/14209931">
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.136">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>UDP-N-acetylglucosamine 6-dehydrogenase</skos:prefLabel>
<skos:altLabel>UDP-2-acetamido-2-deoxy-D-glucose:NAD oxidoreductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.136#SIPB9569B89A87A6F91"/>
<rdfs:comment>This enzyme participates in the biosynthetic pathway for UDP-alpha-D-ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-mannuronic acid), an important precursor of B-band lipopolysaccharide.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/4312076"/>
<citation rdf:resource="http://purl.uniprot.org/citations/15226302"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.136#SIPB9569B89A87A6F91">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>H2O + 2 NAD(+) + UDP-N-acetyl-alpha-D-glucosamine = 3 H(+) + 2 NADH + UDP-N-2-acetamido-2-deoxy-alpha-D-glucuronate.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.137">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>ribitol-5-phosphate 2-dehydrogenase</skos:prefLabel>
<skos:altLabel>ribitol 5-phosphate dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.137#SIPAF3C466C85A3061A"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.137#SIP80D5424E9AEBB9F9"/>
<rdfs:comment>The enzyme, characterized from the bacterium Lactobacillus plantarum, can use both NAD(+) and NADP(+) as electron acceptor (cf. EC 1.1.1.405).</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/13948358"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.137#SIPAF3C466C85A3061A">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-ribitol 5-phosphate + NADP(+) = D-ribulose 5-phosphate + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.137#SIP80D5424E9AEBB9F9">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-ribitol 5-phosphate + NAD(+) = D-ribulose 5-phosphate + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.138">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>mannitol 2-dehydrogenase (NADP(+))</skos:prefLabel>
<skos:altLabel>NADP-dependent mannitol dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.138#SIP359F9513808A2BD8"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.138#SIP359F9513808A2BD8">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-mannitol + NADP(+) = D-fructose + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.139">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<obsolete rdf:datatype="http://www.w3.org/2001/XMLSchema#boolean">true</obsolete>
<replacedBy rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.21"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.140">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>sorbitol-6-phosphate 2-dehydrogenase</skos:prefLabel>
<skos:altLabel>glucitol-6-phosphate dehydrogenase</skos:altLabel>
<skos:altLabel>ketosephosphate reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.140#SIP7EADE121E0CF0A8C"/>
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<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.140#SIP7EADE121E0CF0A8C">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-sorbitol 6-phosphate + NAD(+) = beta-D-fructose 6-phosphate + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.141">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>15-hydroxyprostaglandin dehydrogenase (NAD(+))</skos:prefLabel>
<skos:altLabel>15-hydroxyprostaglandin dehydrogenase</skos:altLabel>
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<rdfs:comment>Acts on prostaglandins E2, F2alpha and B1, but not on prostaglandin D2 (cf. EC 1.1.1.196 and EC 1.1.1.197).</rdfs:comment>
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<citation rdf:resource="http://purl.uniprot.org/citations/803247"/>
<citation rdf:resource="http://purl.uniprot.org/citations/1117007"/>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>NAD(+) + prostaglandin E2 = 15-oxoprostaglandin E2 + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.142">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>D-pinitol dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.142#SIP79328FED8E47F0D1"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.142#SIP79328FED8E47F0D1">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>5D-5-O-methyl-chiro-inositol + NADP(+) = 2D-5-O-methyl-2,3,5/4,6-pentahydroxycyclohexanone + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/4389340">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/4389340"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/4389340"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.143">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>sequoyitol dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.143#SIP56F2FE943AE8AE64"/>
<citation rdf:resource="http://purl.uniprot.org/citations/4389340"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.143#SIP56F2FE943AE8AE64">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>1D-5-O-methyl-myo-inositol + NAD(+) = 2D-5-O-methyl-2,3,5/4,6-pentahydroxycyclohexanone + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/4389340">
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.144">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>perillyl-alcohol dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.144#SIP1B1A8C90182282AF"/>
<rdfs:comment>Oxidizes a number of primary alcohols with the alcohol group allylic to an endocyclic double bond and a 6-membered ring, either aromatic or hydroaromatic.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/4289759"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.144#SIP1B1A8C90182282AF">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>NAD(+) + perillyl alcohol = H(+) + NADH + perillyl aldehyde.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.145">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>3beta-hydroxy-Delta(5)-steroid dehydrogenase</skos:prefLabel>
<skos:altLabel>3beta-hydroxy-5-ene steroid dehydrogenase</skos:altLabel>
<skos:altLabel>progesterone reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.145#SIP60EAE486E8A4BB44"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.145#SIPB59E23537E74CD67"/>
<rdfs:comment>Acts on 3beta-hydroxyandrost-5-en-17-one to form androst-4-ene-3,17-dione and on 3beta-hydroxypregn-5-en-20-one to form progesterone.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/4226148"/>
<citation rdf:resource="http://purl.uniprot.org/citations/14220672"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.145#SIP60EAE486E8A4BB44">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>a 3beta-hydroxy-Delta(5)-steroid + NAD(+) = a 3-oxo-Delta(5)-steroid + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.145#SIPB59E23537E74CD67">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>3beta-hydroxyandrost-5-en-17-one + NAD(+) = androst-5-ene-3,17-dione + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/4226148">
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.146">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>11beta-hydroxysteroid dehydrogenase</skos:prefLabel>
<skos:altLabel>corticosteroid 11beta-dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.146#SIPC3E51EE1CF8CB1A6"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.146#SIPC3E51EE1CF8CB1A6">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>an 11beta-hydroxysteroid + NADP(+) = an 11-oxosteroid + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/2661206">
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<rdf:Description rdf:about="http://purl.uniprot.org/citations/2808402">
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<rdf:Description rdf:about="http://purl.uniprot.org/citations/3139396">
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.147">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>16alpha-hydroxysteroid dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.147#SIP8C96C061421D6610"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.147#SIP3DD46FB1FE5CF8D7"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.147#SIP8C96C061421D6610">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>a 16alpha-hydroxysteroid + NADP(+) = a 16-oxosteroid + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.147#SIP3DD46FB1FE5CF8D7">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>a 16alpha-hydroxysteroid + NAD(+) = a 16-oxosteroid + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.148">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>estradiol 17alpha-dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.148#SIP813A774B03AD8C59"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.148#SIPAD78D48BCC71D5E0"/>
<citation rdf:resource="http://purl.uniprot.org/citations/4383682"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.148#SIP813A774B03AD8C59">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>17alpha-estradiol + NAD(+) = estrone + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.148#SIPAD78D48BCC71D5E0">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>17alpha-estradiol + NADP(+) = estrone + H(+) + NADPH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.149">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>20alpha-hydroxysteroid dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.149#SIP99A4A7AC7FD4C194"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.149#SIP5A784845E491C2F0"/>
<rdfs:comment>Re-specific with respect to NAD(P)(+) (cf. EC 1.1.1.62).</rdfs:comment>
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<citation rdf:resource="http://purl.uniprot.org/citations/6935192"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.149#SIP99A4A7AC7FD4C194">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(17R,20S)-17,20-dihydroxypregn-4-en-3-one + NAD(+) = 17alpha-hydroxyprogesterone + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.149#SIP5A784845E491C2F0">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(17R,20S)-17,20-dihydroxypregn-4-en-3-one + NADP(+) = 17alpha-hydroxyprogesterone + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/4382486">
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.150">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>21-hydroxysteroid dehydrogenase (NAD(+))</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.150#SIP8C3B65BF93F648C5"/>
<rdfs:comment>Acts on a number of 21-hydroxycorticosteroids.</rdfs:comment>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.150#SIP8C3B65BF93F648C5">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>NAD(+) + pregnan-21-ol = H(+) + NADH + pregnan-21-al.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.151">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>21-hydroxysteroid dehydrogenase (NADP(+))</skos:prefLabel>
<skos:altLabel>21-hydroxy steroid (nicotinamide adenine dinucleotide phosphate) dehydrogenase</skos:altLabel>
<skos:altLabel>21-hydroxy steroid dehydrogenase</skos:altLabel>
<skos:altLabel>21-hydroxy steroid dehydrogenase (nicotinamide adenine dinucleotide phosphate)</skos:altLabel>
<skos:altLabel>NADP-21-hydroxysteroid dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.151#SIP43FEF5D1E60C9636"/>
<rdfs:comment>Acts on a number of 21-hydroxycorticosteroids.</rdfs:comment>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.151#SIP43FEF5D1E60C9636">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>NADP(+) + pregnan-21-ol = H(+) + NADPH + pregnan-21-al.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.152">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>3alpha-hydroxy-5beta-androstane-17-one 3alpha-dehydrogenase</skos:prefLabel>
<skos:altLabel>etiocholanolone 3alpha-dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.152#SIPF59C7CB2C770D54A"/>
<citation rdf:resource="http://purl.uniprot.org/citations/5365796"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.152#SIPF59C7CB2C770D54A">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>3alpha-hydroxy-5beta-androstan-17-one + NAD(+) = 5beta-androstane-3,17-dione + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.153">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming)</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.153#SIPD53064D42535ED28"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.153#SIP21EA30C5F9D44608"/>
<rdfs:comment>This enzyme catalyzes the final step in the de novo synthesis of tetrahydrobiopterin from GTP.</rdfs:comment>
<rdfs:comment>The enzyme, which is found in higher animals and some fungi and bacteria, produces the erythro form of tetrahydrobiopterin.</rdfs:comment>
<rdfs:comment>Cf. EC 1.1.1.325.</rdfs:comment>
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<rdfs:label>(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + 2 NADP(+) = 6-pyruvoyl-5,6,7,8-tetrahydropterin + 2 H(+) + 2 NADPH.</rdfs:label>
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<rdfs:label>(S)-ureidoglycolate + NAD(+) = H(+) + N-carbamoyl-2-oxoglycine + NADH.</rdfs:label>
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<rdfs:label>(S)-ureidoglycolate + NADP(+) = H(+) + N-carbamoyl-2-oxoglycine + NADPH.</rdfs:label>
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<skos:prefLabel>glycerol 2-dehydrogenase (NADP(+))</skos:prefLabel>
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<rdfs:label>glycerol + NADP(+) = dihydroxyacetone + H(+) + NADPH.</rdfs:label>
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<skos:prefLabel>3-hydroxybutyryl-CoA dehydrogenase</skos:prefLabel>
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<skos:altLabel>BHBD</skos:altLabel>
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<rdfs:label>(3S)-3-hydroxybutanoyl-CoA + NADP(+) = acetoacetyl-CoA + H(+) + NADPH.</rdfs:label>
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<skos:prefLabel>7alpha-hydroxysteroid dehydrogenase</skos:prefLabel>
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<rdfs:comment>Catalyzes the oxidation of the 7alpha-hydroxy group of bile acids and alcohols both in their free and conjugated forms.</rdfs:comment>
<rdfs:comment>The Bacteroides fragilis and Clostridium enzymes can also utilize NADP(+).</rdfs:comment>
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<rdfs:label>cholate + NAD(+) = 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + H(+) + NADH.</rdfs:label>
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<skos:prefLabel>dihydrobunolol dehydrogenase</skos:prefLabel>
<skos:altLabel>bunolol reductase</skos:altLabel>
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<rdfs:comment>Also acts, more slowly, with NAD(+).</rdfs:comment>
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<rdfs:label>dihydrobunolol + NADP(+) = bunolol + H(+) + NADPH.</rdfs:label>
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<skos:prefLabel>erythrulose reductase</skos:prefLabel>
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<rdfs:comment>NAD(+) is also utilized, but more slowly.</rdfs:comment>
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<rdfs:label>D-threitol + NADP(+) = D-erythrulose + H(+) + NADPH.</rdfs:label>
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<skos:prefLabel>cyclopentanol dehydrogenase</skos:prefLabel>
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<rdfs:comment>4-Methylcyclohexanol and cyclohexanol can also act as substrates.</rdfs:comment>
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<rdfs:label>cyclopentanol + NAD(+) = cyclopentanone + H(+) + NADH.</rdfs:label>
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<skos:prefLabel>hexadecanol dehydrogenase</skos:prefLabel>
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<rdfs:comment>The liver enzyme acts on long-chain alcohols from C8 to C16.</rdfs:comment>
<rdfs:comment>The Euglena enzyme also oxidizes the corresponding aldehydes to fatty acids.</rdfs:comment>
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<rdfs:label>hexadecan-1-ol + NAD(+) = H(+) + hexadecanal + NADH.</rdfs:label>
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<skos:prefLabel>2-alkyn-1-ol dehydrogenase</skos:prefLabel>
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<rdfs:comment>Acts on a variety of 2-alkyn-1-ols, and also on 1,4-butanediol.</rdfs:comment>
<rdfs:comment>NADP(+) also acts as acceptor, but more slowly.</rdfs:comment>
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<rdfs:label>2-butyne-1,4-diol + NAD(+) = 4-hydroxy-2-butynal + H(+) + NADH.</rdfs:label>
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<skos:prefLabel>hydroxycyclohexanecarboxylate dehydrogenase</skos:prefLabel>
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<rdfs:comment>Acts on hydroxycyclohexanecarboxylates that have an equatorial carboxy group at C-1, an axial hydroxy group at C-3 and an equatorial hydroxy or carbonyl group at C-4, including (-)-quinate and (-)-shikimate.</rdfs:comment>
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<rdfs:label>(1S,3R,4S)-3,4-dihydroxycyclohexane-1-carboxylate + NAD(+) = (1S,4S)-4-hydroxy-3-oxocyclohexane-1-carboxylate + H(+) + NADH.</rdfs:label>
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<skos:prefLabel>hydroxymalonate dehydrogenase</skos:prefLabel>
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<rdfs:label>hydroxymalonate + NAD(+) = H(+) + NADH + oxomalonate.</rdfs:label>
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<skos:prefLabel>2-dehydropantolactone reductase (Re-specific)</skos:prefLabel>
<skos:altLabel>2-dehydropantolactone reductase (A-specific)</skos:altLabel>
<skos:altLabel>2-dehydropantoyl-lactone reductase (A-specific)</skos:altLabel>
<skos:altLabel>2-ketopantoyl lactone reductase</skos:altLabel>
<skos:altLabel>ketopantoyl lactone reductase</skos:altLabel>
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<rdfs:comment>The enzyme from Saccharomyces cerevisiae differs from that from Escherichia coli (EC 1.1.1.214), which is specific for the Si-face of NADP, and in receptor requirements from EC 1.1.99.26.</rdfs:comment>
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<rdfs:label>(R)-pantolactone + NADP(+) = 2-dehydropantolactone + H(+) + NADPH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.169">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>2-dehydropantoate 2-reductase</skos:prefLabel>
<skos:altLabel>ketopantoate reductase</skos:altLabel>
<skos:altLabel>ketopantoic acid reductase</skos:altLabel>
<skos:altLabel>KPA reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.169#SIPEAD5A43400457C5B"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.169#SIPEAD5A43400457C5B">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.170">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>3beta-hydroxysteroid-4alpha-carboxylate 3-dehydrogenase (decarboxylating)</skos:prefLabel>
<skos:altLabel>3beta-hydroxy-4alpha-methylcholestenecarboxylate 3-dehydrogenase (decarboxylating)</skos:altLabel>
<skos:altLabel>3beta-hydroxy-4beta-methylcholestenecarboxylate 3-dehydrogenase (decarboxylating)</skos:altLabel>
<skos:altLabel>3beta-hydroxy-4beta-methylcholestenoate dehydrogenase</skos:altLabel>
<skos:altLabel>sterol-4alpha-carboxylate 3-dehydrogenase (decarboxylating)</skos:altLabel>
<skos:altLabel>sterol 4alpha-carboxylic decarboxylase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.170#SIPC5129D9E36A50F90"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.170#SIP6A7D2522E1277DA3"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.170#SIP651682922EA504D4"/>
<rdfs:comment>The enzyme participates in the biosynthesis of several important sterols such as ergosterol and cholesterol.</rdfs:comment>
<rdfs:comment>It is part of a three enzyme system that removes methyl groups from the C-4 position of steroid molecules.</rdfs:comment>
<rdfs:comment>The first enzyme, EC 1.14.18.9, catalyzes three successive oxidations of the methyl group, resulting in a carboxyl group; the second enzyme, EC 1.1.1.170, catalyzes an oxidative decarboxylation that results in a reduction of the 3beta-hydroxy group at the C-3 carbon to an oxo group; and the last enzyme, EC 1.1.1.270, reduces the 3-oxo group back to a 3beta-hydroxyl.</rdfs:comment>
<rdfs:comment>If a second methyl group remains at the C-4 position, this enzyme also catalyzes its epimerization from 4beta to 4alpha orientation, so it could serve as a substrate for a second round of demethylation.</rdfs:comment>
<rdfs:comment>Cf. EC 1.1.1.418.</rdfs:comment>
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<rdfs:label>a 3beta-hydroxysteroid-4alpha-carboxylate + NADP(+) = a 3-oxosteroid + CO2 + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.170#SIP6A7D2522E1277DA3">
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<rdfs:label>a 3beta-hydroxysteroid-4alpha-carboxylate + NAD(+) = a 3-oxosteroid + CO2 + NADH.</rdfs:label>
</rdf:Description>
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<rdfs:label>4beta-methylzymosterol-4alpha-carboxylate + NADP(+) = 3-dehydro-4-methylzymosterol + CO2 + NADPH.</rdfs:label>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.171">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<obsolete rdf:datatype="http://www.w3.org/2001/XMLSchema#boolean">true</obsolete>
<replacedBy rdf:resource="http://purl.uniprot.org/enzyme/1.5.1.20"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.172">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>2-oxoadipate reductase</skos:prefLabel>
<skos:altLabel>2-ketoadipate reductase</skos:altLabel>
<skos:altLabel>alpha-ketoadipate reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.172#SIP74D0754BA2FCB584"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.172#SIP74D0754BA2FCB584">
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<rdfs:label>2-hydroxyadipate + NAD(+) = 2-oxoadipate + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.173">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>L-rhamnose 1-dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.173#SIP3A5089B26BC560B2"/>
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<rdfs:label>L-rhamnofuranose + NAD(+) = H(+) + L-rhamnono-1,4-lactone + NADH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.174">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>cyclohexane-1,2-diol dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.174#SIP3A4A0BE219851E68"/>
<rdfs:comment>Also oxidizes, more slowly, the cis isomer and 2-hydroxycyclohexanone.</rdfs:comment>
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<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdfs:label>NAD(+) + trans-cyclohexane-1,2-diol = 2-hydroxycyclohexan-1-one + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.175">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>D-xylose 1-dehydrogenase</skos:prefLabel>
<skos:altLabel>D-xylose dehydrogenase</skos:altLabel>
<skos:altLabel>NAD-D-xylose dehydrogenase</skos:altLabel>
<skos:altLabel>NAD-linked D-xylose dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.175#SIP0B4932267B364C4E"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.175#SIP0B4932267B364C4E">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-xylose + NAD(+) = D-xylono-1,5-lactone + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.176">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>12alpha-hydroxysteroid dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.176#SIP01F798E8F8D26263"/>
<rdfs:comment>Catalyzes the oxidation of the 12alpha-hydroxy group of bile acids, both in their free and conjugated form.</rdfs:comment>
<rdfs:comment>Also acts on bile alcohols.</rdfs:comment>
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<rdfs:label>cholate + NADP(+) = 3alpha,7alpha-dihydroxy-12-oxo-5beta-cholanate + H(+) + NADPH.</rdfs:label>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.177">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>glycerol-3-phosphate 1-dehydrogenase (NADP(+))</skos:prefLabel>
<skos:altLabel>glycerin-3-phosphate dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.177#SIPD7ADAA50F603340D"/>
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<rdfs:label>NADP(+) + sn-glycerol 3-phosphate = D-glyceraldehyde 3-phosphate + H(+) + NADPH.</rdfs:label>
</rdf:Description>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>3-hydroxy-2-methylbutyryl-CoA dehydrogenase</skos:prefLabel>
<skos:altLabel>2-methyl-3-hydroxybutyryl-CoA dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.178#SIP908401D359B16371"/>
<rdfs:comment>Also acts, more slowly, on (2S,3S)-2-hydroxy-3-methylpentanoyl-CoA.</rdfs:comment>
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<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdfs:label>(2S,3S)-3-hydroxy-2-methylbutanoyl-CoA + NAD(+) = 2-methyl-3-oxobutanoyl-CoA + H(+) + NADH.</rdfs:label>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>D-xylose 1-dehydrogenase (NADP(+), D-xylono-1,5-lactone-forming)</skos:prefLabel>
<skos:altLabel>D-xylose-NADP dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.179#SIPAA81FD84D1AB7017"/>
<rdfs:comment>The enzyme, characterized from pig arterial vessels and eye lens, also acts, more slowly, on L-arabinose and D-ribose.</rdfs:comment>
<rdfs:comment>Cf. EC 1.1.1.424.</rdfs:comment>
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<rdfs:label>D-xylose + NADP(+) = D-xylono-1,5-lactone + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.180">
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<obsolete rdf:datatype="http://www.w3.org/2001/XMLSchema#boolean">true</obsolete>
<replacedBy rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.131"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.181">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>cholest-5-ene-3beta,7alpha-diol 3beta-dehydrogenase</skos:prefLabel>
<skos:altLabel>3beta-hydroxy-Delta(5)-C27-steroid oxidoreductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.181#SIPF8E77B79371766B3"/>
<rdfs:comment>Highly specific for 3beta-hydroxy-C27-steroids with Delta(5)-double bond.</rdfs:comment>
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<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdfs:label>7alpha-hydroxycholesterol + NAD(+) = 7alpha-hydroxycholest-4-en-3-one + H(+) + NADH.</rdfs:label>
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<skos:prefLabel>geraniol dehydrogenase (NADP(+))</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.183#SIP9375268EAAD41A52"/>
<rdfs:comment>Also acts, more slowly on farnesol but not on nerol.</rdfs:comment>
<rdfs:comment>The enzyme produces a mixture known as citral, which includes geranial and neral.</rdfs:comment>
<rdfs:comment>It is still not known whether neral is produced directly by the enzyme, or by isomerization of geranial.</rdfs:comment>
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<rdfs:label>(2E)-geraniol + NADP(+) = (2E)-geranial + H(+) + NADPH.</rdfs:label>
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<skos:prefLabel>carbonyl reductase (NADPH)</skos:prefLabel>
<skos:altLabel>aldehyde reductase I</skos:altLabel>
<skos:altLabel>NADPH-dependent carbonyl reductase</skos:altLabel>
<skos:altLabel>prostaglandin 9-ketoreductase</skos:altLabel>
<skos:altLabel>xenobiotic ketone reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.184#SIPD3F01639DC45DCBC"/>
<rdfs:comment>Acts on a wide range of carbonyl compounds, including quinones, aromatic aldehydes, ketoaldehydes, daunorubicin, and prostaglandins E and F, reducing them to the corresponding alcohol.</rdfs:comment>
<rdfs:comment>Si-specific with respect to NADPH (cf. EC 1.1.1.2).</rdfs:comment>
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<citation rdf:resource="http://purl.uniprot.org/citations/7005231"/>
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<rdfs:label>a secondary alcohol + NADP(+) = a ketone + H(+) + NADPH.</rdfs:label>
</rdf:Description>
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<skos:prefLabel>L-glycol dehydrogenase</skos:prefLabel>
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<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.185#SIPDD5FFE22F2EC3BC3"/>
<rdfs:comment>The 2-hydroxycarbonyl compound formed can be further oxidized to a vicinal dicarbonyl compound.</rdfs:comment>
<rdfs:comment>In the reverse direction, vicinal diketones, glyceraldehyde, glyoxal, methylglyoxal, 2-oxo-hydroxyketones and 2-ketoacid esters can be reduced.</rdfs:comment>
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<rdfs:label>an L-glycol + NADP(+) = a 2-hydroxycarbonyl + H(+) + NADPH.</rdfs:label>
</rdf:Description>
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<rdfs:label>an L-glycol + NAD(+) = a 2-hydroxycarbonyl + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>dTDP-galactose 6-dehydrogenase</skos:prefLabel>
<skos:altLabel>thymidine-diphosphate-galactose dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.186#SIP3F3BF4C882D2D1CC"/>
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<rdfs:label>dTDP-D-galactose + H2O + 2 NADP(+) = dTDP-D-galacturonate + 3 H(+) + 2 NADPH.</rdfs:label>
</rdf:Description>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>GDP-4-dehydro-D-rhamnose reductase</skos:prefLabel>
<skos:altLabel>GDP-4-keto-6-deoxy-D-mannose reductase</skos:altLabel>
<skos:altLabel>GDP-4-keto-D-rhamnose reductase</skos:altLabel>
<skos:altLabel>guanosine diphosphate-4-keto-D-rhamnose reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.187#SIPF8A6D6C776F30998"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.187#SIP8D775DDCDC45B1A0"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.187#SIP745EEB7F5739C476"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.187#SIPBB803B5B08738979"/>
<rdfs:comment>The enzyme, which operates in the opposite direction to that shown, forms a mixture of GDP-alpha-D-rhamnose and its C-4 epimer, GDP-6-deoxy-alpha-D-talose.</rdfs:comment>
<rdfs:comment>Cf. EC 1.1.1.281 and EC 1.1.1.135.</rdfs:comment>
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<rdfs:label>GDP-alpha-D-rhamnose + NAD(+) = GDP-4-dehydro-alpha-D-rhamnose + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdfs:label>GDP-alpha-D-rhamnose + NADP(+) = GDP-4-dehydro-alpha-D-rhamnose + H(+) + NADPH.</rdfs:label>
</rdf:Description>
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<rdfs:label>GDP-6-deoxy-alpha-D-talose + NADP(+) = GDP-4-dehydro-alpha-D-rhamnose + H(+) + NADPH.</rdfs:label>
</rdf:Description>
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<rdfs:label>GDP-6-deoxy-alpha-D-talose + NAD(+) = GDP-4-dehydro-alpha-D-rhamnose + H(+) + NADH.</rdfs:label>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>prostaglandin-F synthase</skos:prefLabel>
<skos:altLabel>PGD2 11-ketoreductase</skos:altLabel>
<skos:altLabel>PGF synthetase</skos:altLabel>
<skos:altLabel>prostaglandin 11-ketoreductase</skos:altLabel>
<skos:altLabel>prostaglandin-D2 11-ketoreductase</skos:altLabel>
<skos:altLabel>prostaglandin-D2 11-reductase</skos:altLabel>
<skos:altLabel>prostaglandin-D2 ketoreductase</skos:altLabel>
<skos:altLabel>prostaglandin-F synthetase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.188#SIP3774DD77825DC62D"/>
<rdfs:comment>Reduces prostaglandin D2 and prostaglandin H2 to prostaglandin F2; prostaglandin D2 is not an intermediate in the reduction of prostaglandin H2.</rdfs:comment>
<rdfs:comment>Also catalyzes the reduction of a number of carbonyl compounds, such as 9,10-phenanthroquinone and 4-nitroacetophenone.</rdfs:comment>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>NADP(+) + prostaglandin F2alpha = H(+) + NADPH + prostaglandin D2.</rdfs:label>
</rdf:Description>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>prostaglandin-E2 9-reductase</skos:prefLabel>
<skos:altLabel>9-keto-prostaglandin E2 reductase</skos:altLabel>
<skos:altLabel>9-ketoprostaglandin reductase</skos:altLabel>
<skos:altLabel>PGE2 9-ketoreductase</skos:altLabel>
<skos:altLabel>PGE2 9-oxoreductase</skos:altLabel>
<skos:altLabel>prostaglandin-E2 9-oxoreductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.189#SIP6E81084FD8934FFA"/>
<rdfs:comment>Reduces prostaglandin E2 to prostaglandin F2alpha.</rdfs:comment>
<rdfs:comment>A number of other 9-oxo- and 15-oxo-prostaglandin derivatives can also be reduced to the corresponding hydroxy compounds.</rdfs:comment>
<rdfs:comment>May be identical with EC 1.1.1.197.</rdfs:comment>
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<rdfs:label>NADP(+) + prostaglandin F2alpha = H(+) + NADPH + prostaglandin E2.</rdfs:label>
</rdf:Description>
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<dcterms:identifier>doi:10.1016/s0021-9258(19)41336-7</dcterms:identifier>
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<dcterms:identifier>doi:10.1016/0090-6980(85)90196-0</dcterms:identifier>
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<dcterms:identifier>doi:10.1016/0076-6879(82)86178-8</dcterms:identifier>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>indole-3-acetaldehyde reductase (NADH)</skos:prefLabel>
<skos:altLabel>indoleacetaldehyde reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.190#SIPCBE046A60D90A955"/>
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<rdfs:label>indole-3-ethanol + NAD(+) = H(+) + indole-3-acetaldehyde + NADH.</rdfs:label>
</rdf:Description>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>indole-3-acetaldehyde reductase (NADPH)</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.191#SIP88EB3F3EB7939E41"/>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>indole-3-ethanol + NADP(+) = H(+) + indole-3-acetaldehyde + NADPH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.192">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>long-chain-alcohol dehydrogenase</skos:prefLabel>
<skos:altLabel>fatty alcohol oxidoreductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.192#SIP6E87F05D6A16C45F"/>
<rdfs:comment>Hexadecanol is a good substrate.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/34610"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.192#SIP6E87F05D6A16C45F">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>a long-chain primary fatty alcohol + H2O + 2 NAD(+) = a long-chain fatty acid + 3 H(+) + 2 NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/34610">
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.193">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>5-amino-6-(5-phosphoribosylamino)uracil reductase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.193#SIP22E1C354B1D5B94C"/>
<citation rdf:resource="http://purl.uniprot.org/citations/30756"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.193#SIP22E1C354B1D5B94C">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>5-amino-6-(5-phospho-D-ribitylamino)uracil + NADP(+) = 5-amino-6-(5-phospho-D-ribosylamino)uracil + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/30756">
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.194">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>coniferyl-alcohol dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.194#SIPC5C11EEF3693297D"/>
<rdfs:comment>Specific for coniferyl alcohol; does not act on cinnamyl alcohol, 4-coumaryl alcohol or sinapyl alcohol.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/1250"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.194#SIPC5C11EEF3693297D">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(E)-coniferol + NADP(+) = (E)-coniferaldehyde + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/1250">
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.195">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>cinnamyl-alcohol dehydrogenase</skos:prefLabel>
<skos:altLabel>CAD</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.195#SIP64D63040884140E4"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.195#SIP0A36BCD13CEA515C"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.195#SIPC5C11EEF3693297D"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.195#SIP06001949B73AAF8C"/>
<rdfs:comment>Acts on coniferyl alcohol, sinapyl alcohol, 4-coumaryl alcohol and cinnamyl alcohol (cf. EC 1.1.1.194).</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/1250"/>
<citation rdf:resource="http://purl.uniprot.org/citations/572771"/>
<citation rdf:resource="http://purl.uniprot.org/citations/6365550"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.195#SIP64D63040884140E4">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(E)-cinnamyl alcohol + NADP(+) = (E)-cinnamaldehyde + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.195#SIP0A36BCD13CEA515C">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(E)-sinapyl alcohol + NADP(+) = (E)-sinapaldehyde + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.195#SIPC5C11EEF3693297D">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(E)-coniferol + NADP(+) = (E)-coniferaldehyde + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.195#SIP06001949B73AAF8C">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(E)-4-coumaroyl alcohol + NADP(+) = (E)-4-coumaraldehyde + H(+) + NADPH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/citations/6365550">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.196">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>15-hydroxyprostaglandin-D dehydrogenase (NADP(+))</skos:prefLabel>
<skos:altLabel>prostaglandin-D 15-dehydrogenase (NADP(+))</skos:altLabel>
<skos:altLabel>prostaglandin-D 15-dehydrogenase (NADP+)</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.196#SIP2C275C95275B3558"/>
<rdfs:comment>Specific for prostaglandins D (cf. EC 1.1.1.141 and EC 1.1.1.197).</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/7354056"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.196#SIP2C275C95275B3558">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>NADP(+) + prostaglandin D2 = 15-oxoprostaglandin D2 + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/7354056">
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.197">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>15-hydroxyprostaglandin dehydrogenase (NADP(+))</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.197#SIP9182919ABE511424"/>
<rdfs:comment>Acts on prostaglandins E2, F2alpha and B1, but not on prostaglandin D2 (cf. EC 1.1.1.141 and EC 1.1.1.196).</rdfs:comment>
<rdfs:comment>May be identical with EC 1.1.1.189.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/234431"/>
<citation rdf:resource="http://purl.uniprot.org/citations/10803247"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.197#SIP9182919ABE511424">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>NADP(+) + prostaglandin E1 = 15-oxoprostaglandin E1 + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/234431">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.198">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<replaces rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.182"/>
<skos:prefLabel>(+)-borneol dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.198#SIP372AE2B152C5EDDB"/>
<rdfs:comment>NADP(+) can also act, more slowly.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/677891"/>
<citation rdf:resource="http://purl.uniprot.org/citations/3310901"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.198#SIP372AE2B152C5EDDB">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(1R,2S,4R)-borneol + NAD(+) = (1R,4R)-camphor + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/677891">
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<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/677891"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/citations/3310901">
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.199">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>(S)-usnate reductase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.199#SIP563DCC2768565373"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.199#SIP563DCC2768565373">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(6R)-2-acetyl-6-(3-acetyl-2,4,6-trihydroxy-5-methylphenyl)-3-hydroxy-6-methylcyclohexa-2,4-dien-1-one + NAD(+) = (S)-usnate + 2 H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.200">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>aldose-6-phosphate reductase (NADPH)</skos:prefLabel>
<skos:altLabel>NADP-dependent D-sorbitol-6-phosphate dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.200#SIP5F453F725C01D4A9"/>
<rdfs:comment>In the reverse reaction, acts also on D-galactose 6-phosphate and, more slowly, on D-mannose 6-phosphate and 2-deoxy-D-glucose 6-phosphate.</rdfs:comment>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.200#SIP5F453F725C01D4A9">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-sorbitol 6-phosphate + NADP(+) = aldehydo-D-glucose 6-phosphate + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.201">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>7beta-hydroxysteroid dehydrogenase (NADP(+))</skos:prefLabel>
<skos:altLabel>NADP-dependent 7beta-hydroxysteroid dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.201#SIPFA4364575379423E"/>
<rdfs:comment>Catalyzes the oxidation of the 7beta-hydroxy group of bile acids such as ursodeoxycholate.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/6758698"/>
<citation rdf:resource="http://purl.uniprot.org/citations/6945134"/>
<citation rdf:resource="http://purl.uniprot.org/citations/6954878"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.201#SIPFA4364575379423E">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>a 7beta-hydroxysteroid + NADP(+) = a 7-oxosteroid + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/6758698">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/citations/6945134">
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.202">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>1,3-propanediol dehydrogenase</skos:prefLabel>
<skos:altLabel>1,3-propanediol oxidoreductase</skos:altLabel>
<skos:altLabel>3-hydroxypropionaldehyde reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.202#SIP8A288C27C3957DB7"/>
<citation rdf:resource="http://purl.uniprot.org/citations/7035429"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.202#SIP8A288C27C3957DB7">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>NAD(+) + propane-1,3-diol = 3-hydroxypropanal + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.203">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<replaces rdf:resource="http://purl.uniprot.org/enzyme/1.2.1.35"/>
<skos:prefLabel>uronate dehydrogenase</skos:prefLabel>
<skos:altLabel>uronic acid dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.203#SIPCCD3FF04300C7B72"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.203#SIPD32BBA687EEE3AF1"/>
<rdfs:comment>The enzyme, characterized from the bacterium Agrobacterium fabrum, participates in oxidative degradation pathways for galacturonate and glucuronate.</rdfs:comment>
<rdfs:comment>The enzyme can only accept the beta anomeric form of the substrate.</rdfs:comment>
<rdfs:comment>The 1,5 lactone product is rather stable at cytosolic pH and does not hydrolyze spontaneously at a substantial rate.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/13657147"/>
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<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.203#SIPCCD3FF04300C7B72">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>beta-D-galacturonate + NAD(+) = D-galactaro-1,5-lactone + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.203#SIPD32BBA687EEE3AF1">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>beta-D-glucuronate + NAD(+) = D-glucaro-1,5-lactone + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/21676870"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/22493433">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/22493433"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/22493433"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.204">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<obsolete rdf:datatype="http://www.w3.org/2001/XMLSchema#boolean">true</obsolete>
<replacedBy rdf:resource="http://purl.uniprot.org/enzyme/1.17.1.4"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.205">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<replaces rdf:resource="http://purl.uniprot.org/enzyme/1.2.1.14"/>
<skos:prefLabel>IMP dehydrogenase</skos:prefLabel>
<skos:altLabel>IMP oxidoreductase</skos:altLabel>
<skos:altLabel>inosinate dehydrogenase</skos:altLabel>
<skos:altLabel>inosine 5'-monophosphate dehydrogenase</skos:altLabel>
<skos:altLabel>inosine monophosphate oxidoreductase</skos:altLabel>
<skos:altLabel>inosinic acid dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.205#SIP36E06EA0B0332436"/>
<rdfs:comment>The enzyme acts on the hydroxy group of the hydrated derivative of the substrate.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/13428767"/>
<citation rdf:resource="http://purl.uniprot.org/citations/13778733"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.205#SIP36E06EA0B0332436">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>H2O + IMP + NAD(+) = H(+) + NADH + XMP.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/13428767">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/13428767"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/13778733">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/13778733"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/13778733"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.206">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>tropinone reductase I</skos:prefLabel>
<skos:altLabel>TR-I</skos:altLabel>
<skos:altLabel>tropine dehydrogenase</skos:altLabel>
<skos:altLabel>tropinone reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.206#SIP45A80F5E5D08DEF6"/>
<rdfs:comment>Also oxidizes other tropan-3alpha-ols, but not the corresponding beta-derivatives.</rdfs:comment>
<rdfs:comment>Represents, along with EC 1.1.1.236, a branch point in tropane alkaloid metabolism.</rdfs:comment>
<rdfs:comment>Tropine (the product of EC 1.1.1.206) is incorporated into hyoscyamine and scopolamine whereas pseudotropine (the product of EC 1.1.1.236) is the first specific metabolite on the pathway to the calystegines.</rdfs:comment>
<rdfs:comment>Both enzymes are always found together in any given tropane-alkaloid-producing species, have a common substrate, tropinone, and are strictly stereospecific.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/8415746"/>
<citation rdf:resource="http://purl.uniprot.org/citations/16426652"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.206#SIP45A80F5E5D08DEF6">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>NADP(+) + tropine = H(+) + NADPH + tropinone.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/8415746">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/8415746"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/8415746"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/16426652">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/16426652"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/16426652"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.207">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>(-)-menthol dehydrogenase</skos:prefLabel>
<skos:altLabel>monoterpenoid dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.207#SIP86CFA58C93377B38"/>
<rdfs:comment>Acts on a number of other cyclohexanols and cyclohexenols.</rdfs:comment>
<rdfs:comment>Not identical with EC 1.1.1.208.</rdfs:comment>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.207#SIP86CFA58C93377B38">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(-)-menthol + NADP(+) = (1R,4S)-menthone + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.208">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>(+)-neomenthol dehydrogenase</skos:prefLabel>
<skos:altLabel>monoterpenoid dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.208#SIPAAC5780B423EF82E"/>
<rdfs:comment>Acts on a number of other cyclohexanols and cyclohexenols.</rdfs:comment>
<rdfs:comment>Not identical with EC 1.1.1.207.</rdfs:comment>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.208#SIPAAC5780B423EF82E">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(+)-neomenthol + NADP(+) = (1R,4S)-menthone + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.209">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>3(or 17)alpha-hydroxysteroid dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.209#SIPC3B8F7030F5FDAD9"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.209#SIP9BB84DABEEDEA27A"/>
<rdfs:comment>Acts on the 3alpha-hydroxy group of androgens of the 5alpha-androstane series; and also, more slowly, on the 17alpha-hydroxyl group of both androgenic and estrogenic substrates (cf. EC 1.1.1.51).</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/6955302"/>
<citation rdf:resource="http://purl.uniprot.org/citations/6955303"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.209#SIPC3B8F7030F5FDAD9">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>androsterone + NADP(+) = 5alpha-androstan-3,17-dione + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.209#SIP9BB84DABEEDEA27A">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>androsterone + NAD(+) = 5alpha-androstan-3,17-dione + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/6955302">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/6955302"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/6955302"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/6955303">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/6955303"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/6955303"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.210">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>3beta-(or 20alpha)-hydroxysteroid dehydrogenase</skos:prefLabel>
<skos:altLabel>3-beta-HSD</skos:altLabel>
<skos:altLabel>progesterone reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.210#SIP012DADFF0CE7E6C4"/>
<rdfs:comment>Also acts on 20alpha-hydroxysteroids.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/6958329"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.210#SIP012DADFF0CE7E6C4">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>5alpha-androstane-3beta,17beta-diol + NADP(+) = 17beta-hydroxy-5alpha-androstan-3-one + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/6958329">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/6958329"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/6958329"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.211">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>long-chain-3-hydroxyacyl-CoA dehydrogenase</skos:prefLabel>
<skos:altLabel>beta-hydroxyacyl-CoA dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.211#SIPD18854DA1ED3EEBB"/>
<rdfs:comment>This enzyme was purified from the mitochondrial inner membrane.</rdfs:comment>
<rdfs:comment>The enzyme has a preference for long-chain substrates, and activity with C16 substrates was 6- to 15-fold higher than with C4 substrates (cf. EC 1.1.1.35).</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/7150615"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.211#SIPD18854DA1ED3EEBB">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>a long-chain (3S)-3-hydroxy fatty acyl-CoA + NAD(+) = a long-chain 3-oxo-fatty acyl-CoA + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/7150615">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/7150615"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/7150615"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.212">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>3-oxoacyl-[acyl-carrier-protein] reductase (NADH)</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.212#SIP33F11149AA8C5046"/>
<rdfs:comment>Forms part of the fatty acid synthase system in plants.</rdfs:comment>
<rdfs:comment>Can be separated from EC 1.1.1.100.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/7075600"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.212#SIP33F11149AA8C5046">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>a (3R)-hydroxyacyl-[ACP] + NAD(+) = a 3-oxoacyl-[ACP] + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/7075600">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/7075600"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/7075600"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.213">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>3alpha-hydroxysteroid dehydrogenase (Re-specific)</skos:prefLabel>
<skos:altLabel>3alpha-hydroxysteroid dehydrogenase</skos:altLabel>
<skos:altLabel>3alpha-hydroxysteroid dehydrogenase (A-specific)</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.213#SIP0C20651CC5E7FC65"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.213#SIPB73B2D324E3434D2"/>
<rdfs:comment>The enzyme acts on multiple 3alpha-hydroxysteroids.</rdfs:comment>
<rdfs:comment>Re-specific with respect to NAD(+) or NADP(+) (cf. EC 1.1.1.50).</rdfs:comment>
<rdfs:comment>Enzymes whose stereo-specificity with respect to NAD(+) or NADP(+) is not known are described by EC 1.1.1.357.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/4392180"/>
<citation rdf:resource="http://purl.uniprot.org/citations/13278351"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.213#SIP0C20651CC5E7FC65">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>a 3alpha-hydroxysteroid + NAD(+) = a 3-oxosteroid + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.213#SIPB73B2D324E3434D2">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>a 3alpha-hydroxysteroid + NADP(+) = a 3-oxosteroid + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/4392180">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/4392180"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/4392180"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/13278351">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/13278351"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/13278351"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.214">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>2-dehydropantolactone reductase (Si-specific)</skos:prefLabel>
<skos:altLabel>2-dehydropantolactone reductase (B-specific)</skos:altLabel>
<skos:altLabel>2-dehydropantoyl-lactone reductase (B-specific)</skos:altLabel>
<skos:altLabel>2-ketopantoyl lactone reductase</skos:altLabel>
<skos:altLabel>ketopantoyl lactone reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.214#SIPD08E6B969BC8D986"/>
<rdfs:comment>The Escherichia coli enzyme differs from that from Saccharomyces cerevisiae (EC 1.1.1.168), which is specific for the Re-face of NADP, and in receptor requirements from EC 1.1.99.26.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/234966"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.214#SIPD08E6B969BC8D986">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(R)-pantolactone + NADP(+) = 2-dehydropantolactone + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/234966">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/234966"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/234966"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.215">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>gluconate 2-dehydrogenase</skos:prefLabel>
<skos:altLabel>2-keto-D-gluconate reductase</skos:altLabel>
<skos:altLabel>2-ketogluconate reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.215#SIPB44818D90778407E"/>
<rdfs:comment>Also acts on L-idonate, D-galactonate and D-xylonate.</rdfs:comment>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.215#SIPB44818D90778407E">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-gluconate + NADP(+) = 2-dehydro-D-gluconate + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.216">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>farnesol dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.216#SIP75E78A5AE7DEBC53"/>
<rdfs:comment>Also acts, more slowly, on (2Z,6E)-farnesol, geraniol, citronerol and nerol.</rdfs:comment>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.216#SIP75E78A5AE7DEBC53">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(2E,6E)-farnesol + NADP(+) = (2E,6E)-farnesal + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.217">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>benzyl-2-methyl-hydroxybutyrate dehydrogenase</skos:prefLabel>
<skos:altLabel>benzyl 2-methyl-3-hydroxybutyrate dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.217#SIPBC7DA7EA376D285F"/>
<rdfs:comment>Also acts on benzyl (2S,3S)-2-methyl-3-hydroxybutanoate; otherwise highly specific.</rdfs:comment>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.217#SIPBC7DA7EA376D285F">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>benzyl (2R,3S)-2-methyl-3-hydroxybutanoate + NADP(+) = benzyl 2-methyl-3-oxobutanoate + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.218">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>morphine 6-dehydrogenase</skos:prefLabel>
<skos:altLabel>naloxone reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.218#SIP434DA1E5AE8D2B4A"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.218#SIPFA5E6093C403B5A0"/>
<rdfs:comment>Also acts on some other alkaloids, including codeine, normorphine and ethylmorphine, but only very slowly on 7,8-saturated derivatives such as dihydromorphine and dihydrocodeine.</rdfs:comment>
<rdfs:comment>In the reverse direction, also reduces naloxone to the 6alpha-hydroxy analog.</rdfs:comment>
<rdfs:comment>Activated by 2-sulfanylethan-1-ol (2-mercaptoethanol).</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/2580834"/>
<citation rdf:resource="http://purl.uniprot.org/citations/3539118"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.218#SIP434DA1E5AE8D2B4A">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>morphine + NAD(+) = H(+) + morphinone + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.218#SIPFA5E6093C403B5A0">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>morphine + NADP(+) = H(+) + morphinone + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/2580834">
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<rdf:Description rdf:about="http://purl.uniprot.org/citations/3539118">
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.219">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>dihydroflavanol 4-reductase</skos:prefLabel>
<skos:altLabel>dihydroflavonol 4-reductase</skos:altLabel>
<skos:altLabel>dihydrokaempferol 4-reductase</skos:altLabel>
<skos:altLabel>NADPH-dihydromyricetin reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.219#SIP8EAB0EEC51A17EED"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.219#SIPE317F714684E9161"/>
<rdfs:comment>This plant enzyme, involved in the biosynthesis of anthocyanidins, is known to act on (+)-dihydrokaempferol, (+)-taxifolin, and (+)-dihydromyricetin, although some enzymes may act only on a subset of these compounds.</rdfs:comment>
<rdfs:comment>Each dihydroflavonol is reduced to the corresponding cis-flavan-3,4-diol.</rdfs:comment>
<rdfs:comment>NAD(+) can act instead of NADP(+), but more slowly.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/3293532"/>
<citation rdf:resource="http://purl.uniprot.org/citations/16664326"/>
<citation rdf:resource="http://purl.uniprot.org/citations/21701830"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.219#SIP8EAB0EEC51A17EED">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>a (2R,3S,4S)-leucoanthocyanidin + NADP(+) = a (2R,3R)-dihydroflavonol + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.219#SIPE317F714684E9161">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(2R,3S,4S)-3,4-leucopelargonidin + NADP(+) = (2R,3R)-dihydrokaempferol + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/3293532">
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<rdf:Description rdf:about="http://purl.uniprot.org/citations/16664326">
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/21701830">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/21701830"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/21701830"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.220">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>6-pyruvoyltetrahydropterin 2'-reductase</skos:prefLabel>
<skos:altLabel>6PPH4(2'-oxo) reductase</skos:altLabel>
<skos:altLabel>6-pyruvoyl tetrahydropterin (2'-oxo)reductase</skos:altLabel>
<skos:altLabel>6-pyruvoyl-tetrahydropterin 2'-reductase</skos:altLabel>
<skos:altLabel>pyruvoyl-tetrahydropterin reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.220#SIP4C6104B32205E87C"/>
<rdfs:comment>Not identical with EC 1.1.1.153.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/4004850"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.220#SIP4C6104B32205E87C">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>6-lactoyl-5,6,7,8-tetrahydropterin + NADP(+) = 6-pyruvoyl-5,6,7,8-tetrahydropterin + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/4004850">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/4004850"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/4004850"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.221">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>vomifoliol dehydrogenase</skos:prefLabel>
<skos:altLabel>vomifoliol 4'-dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.221#SIP8789ECB1C5AFCD15"/>
<rdfs:comment>Oxidizes vomifoliol to dehydrovomifoliol; involved in the metabolism of abscisic acid in Corynebacterium sp.</rdfs:comment>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.221#SIP8789ECB1C5AFCD15">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(6S,9R)-vomifoliol + NAD(+) = (6S)-6-hydroxy-3-oxo-alpha-ionone + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.222">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<obsolete rdf:datatype="http://www.w3.org/2001/XMLSchema#boolean">true</obsolete>
<replacedBy rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.110"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.223">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>isopiperitenol dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.223#SIP1E7F25D4511303AC"/>
<rdfs:comment>Acts on (-)-trans-isopiperitenol, (+)-trans-piperitenol and (+)-trans-pulegol.</rdfs:comment>
<rdfs:comment>Involved in the biosynthesis of menthol and related monoterpenes in peppermint (Mentha piperita) leaves.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/3885858"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.223#SIP1E7F25D4511303AC">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(1S,6R)-isopiperitenol + NAD(+) = (6R)-isopiperitenone + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/3885858">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/3885858"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/3885858"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.224">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>mannose-6-phosphate 6-reductase</skos:prefLabel>
<skos:altLabel>NADPH-dependent M6P reductase</skos:altLabel>
<skos:altLabel>NADPH-mannose-6-P reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.224#SIP06A81F6B3B7A2F9F"/>
<rdfs:comment>Involved in the biosynthesis of mannitol in celery (Apium graveolens) leaves.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/16663332"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.224#SIP06A81F6B3B7A2F9F">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-mannitol 1-phosphate + NADP(+) = D-mannose 6-phosphate + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/16663332">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/16663332"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/16663332"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.225">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>chlordecone reductase</skos:prefLabel>
<skos:altLabel>CDR</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.225#SIP20AC38D7322516B9"/>
<rdfs:comment>Chlordecone, an organochlorine pesticide, is 1,1a,3,3a,4,5,5a,5b,6-decachlorooctahydro-1,3,4-metheno-2H-cyclobuta[cd]pentalen-2-one.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/2427522"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.225#SIP20AC38D7322516B9">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>chlordecone alcohol + NADP(+) = chlordecone + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/2427522">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/2427522"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.226">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>4-hydroxycyclohexanecarboxylate dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.226#SIP578F89725394ACF8"/>
<rdfs:comment>The enzyme from Corynebacterium cyclohexanicum is highly specific for the trans-4-hydroxy derivative.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/3292236"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.226#SIP578F89725394ACF8">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>NAD(+) + trans-4-hydroxycyclohexanecarboxylate = 4-oxocyclohexanecarboxylate + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/3292236">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/3292236"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/3292236"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.227">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<replaces rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.182"/>
<skos:prefLabel>(-)-borneol dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.227#SIP22BF190320FBC501"/>
<rdfs:comment>NADP(+) can also act, more slowly.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/3310901"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.227#SIP22BF190320FBC501">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(1S,2R,4S)-borneol + NAD(+) = (1S,4S)-camphor + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/3310901">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/3310901"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/3310901"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.228">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<replaces rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.182"/>
<skos:prefLabel>(+)-sabinol dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.228#SIP3842BF9665985C05"/>
<rdfs:comment>NADP(+) can also act, more slowly.</rdfs:comment>
<rdfs:comment>Involved in the biosynthesis of (+)-3-thujone and (-)-3-isothujone.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/3310901"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.228#SIP3842BF9665985C05">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(1S,3R,5S)-sabinol + NAD(+) = (1S,5S)-sabinone + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/3310901">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/3310901"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/3310901"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.229">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>diethyl 2-methyl-3-oxosuccinate reductase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.229#SIPFAE3F1623839F0ED"/>
<rdfs:comment>Also acts on diethyl (2S,3R)-2-methyl-3-hydroxysuccinate; and on the corresponding dimethyl esters.</rdfs:comment>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.229#SIPFAE3F1623839F0ED">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>diethyl (2R,3R)-2-methyl-3-hydroxysuccinate + NADP(+) = diethyl 2-methyl-3-oxosuccinate + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.230">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>3alpha-hydroxyglycyrrhetinate dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.230#SIPE1716F27D2939272"/>
<rdfs:comment>Highly specific to 3alpha-hydroxy derivatives of glycyrrhetinate and its analogs.</rdfs:comment>
<rdfs:comment>Not identical to EC 1.1.1.50.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/3164718"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.230#SIPE1716F27D2939272">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>3alpha-hydroxyglycyrrhetinate + NADP(+) = 3-oxoglycyrrhetinate + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/3164718">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/3164718"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/3164718"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.231">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>15-hydroxyprostaglandin-I dehydrogenase (NADP(+))</skos:prefLabel>
<skos:altLabel>PG I2 dehydrogenase</skos:altLabel>
<skos:altLabel>prostacyclin dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.231#SIPFD5B49AF3CB1E80A"/>
<rdfs:comment>Specific for prostaglandin I2.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/6182444"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.231#SIPFD5B49AF3CB1E80A">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>NADP(+) + prostaglandin I2 = 15-dehydro-prostaglandin I2 + H(+) + NADPH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.232">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>15-hydroxyicosatetraenoate dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.232#SIPDD845DDA7FBE9329"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.232#SIPE527AB2CF8051765"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.232#SIPDD845DDA7FBE9329">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(5Z,8Z,11Z,13E,15S)-hydroxyeicosatetraenoate + NAD(+) = 15-oxo-(5Z,8Z,11Z,13E)-eicosatetraenoate + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.232#SIPE527AB2CF8051765">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(5Z,8Z,11Z,13E,15S)-hydroxyeicosatetraenoate + NADP(+) = 15-oxo-(5Z,8Z,11Z,13E)-eicosatetraenoate + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/3052453">
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.233">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>N-acylmannosamine 1-dehydrogenase</skos:prefLabel>
<skos:altLabel>N-acetyl-D-mannosamine dehydrogenase</skos:altLabel>
<skos:altLabel>N-acyl-D-mannosamine dehydrogenase</skos:altLabel>
<skos:altLabel>N-acylmannosamine dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.233#SIP3FFD7C99AC28B789"/>
<rdfs:comment>Acts on acetyl-D-mannosamine and glycolyl-D-mannosamine.</rdfs:comment>
<rdfs:comment>Highly specific.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/3240988"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.233#SIP3FFD7C99AC28B789">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>an N-acyl-D-mannosamine + NAD(+) = an N-acyl-D-mannosaminolactone + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/3240988">
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.234">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>flavanone 4-reductase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.234#SIPCBBA552D87C9C68F"/>
<rdfs:comment>Involved in the biosynthesis of 3-deoxyanthocyanidins from flavanones such as naringenin or eriodictyol.</rdfs:comment>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.234#SIPCBBA552D87C9C68F">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(2S)-flavan-4-ol + NADP(+) = (2S)-flavanone + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.235">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>8-oxocoformycin reductase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.235#SIPDCE95FA16BBD1BD6"/>
<rdfs:comment>Si-specific with respect to NADPH.</rdfs:comment>
<rdfs:comment>Also reduces 8-oxodeoxy-coformycin to the nucleoside antibiotic deoxycoformycin.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/3052586"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.235#SIPDCE95FA16BBD1BD6">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>coformycin + NADP(+) = 8-oxocoformycin + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/3052586">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.236">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>tropinone reductase II</skos:prefLabel>
<skos:altLabel>pseudotropine forming tropinone reductase</skos:altLabel>
<skos:altLabel>TR-II</skos:altLabel>
<skos:altLabel>tropinone reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.236#SIPCB7C64412122E8A2"/>
<rdfs:comment>Represents, along with EC 1.1.1.206, a branch point in tropane alkaloid metabolism.</rdfs:comment>
<rdfs:comment>Tropine (the product of EC 1.1.1.206) is incorporated into hyoscyamine and scopolamine whereas pseudotropine (the product of EC 1.1.1.236) is the first specific metabolite on the pathway to the calystegines.</rdfs:comment>
<rdfs:comment>Both enzymes are always found together in any given tropane-alkaloid-producing species, have a common substrate, tropinone, and are strictly stereospecific.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/8415746"/>
<citation rdf:resource="http://purl.uniprot.org/citations/16426652"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.236#SIPCB7C64412122E8A2">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>NADP(+) + pseudotropine = H(+) + NADPH + tropinone.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/8415746">
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<rdf:Description rdf:about="http://purl.uniprot.org/citations/16426652">
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.237">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>hydroxyphenylpyruvate reductase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.237#SIPD536FB315BE46EE7"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.237#SIP5590D5860E490B6F"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.237#SIPD49F9DE5A393294D"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.237#SIP2571B17DF27ED810"/>
<rdfs:comment>The enzyme participates in the biosynthesis of rosmarinic acid.</rdfs:comment>
<rdfs:comment>It belongs to the family of D-isomer-specific 2-hydroxyacid dehydrogenases, and prefers NADPH to NADH.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/15284489"/>
<citation rdf:resource="http://purl.uniprot.org/citations/25918800"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.237#SIPD536FB315BE46EE7">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(2R)-2-hydroxy-3-(4-hydroxyphenyl)propanoate + NADP(+) = 3-(4-hydroxyphenyl)pyruvate + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.237#SIP5590D5860E490B6F">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(2R)-2-hydroxy-3-(4-hydroxyphenyl)propanoate + NAD(+) = 3-(4-hydroxyphenyl)pyruvate + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.237#SIPD49F9DE5A393294D">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(2R)-3-(3,4-dihydroxyphenyl)lactate + NAD(+) = 3-(3,4-dihydroxyphenyl)pyruvate + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.237#SIP2571B17DF27ED810">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(2R)-3-(3,4-dihydroxyphenyl)lactate + NADP(+) = 3-(3,4-dihydroxyphenyl)pyruvate + H(+) + NADPH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/citations/29329649">
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.238">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>12beta-hydroxysteroid dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.238#SIP5B9E8A624FAFB6C5"/>
<rdfs:comment>Acts on a number of bile acids, both in their free and conjugated forms.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/3167086"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.238#SIP5B9E8A624FAFB6C5">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>3alpha,7alpha,12beta-trihydroxy-5beta-cholanate + NADP(+) = 3alpha,7alpha-dihydroxy-12-oxo-5beta-cholanate + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/3167086">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/3167086"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/3167086"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.239">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<replaces rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.63"/>
<skos:prefLabel>3alpha-(17beta)-hydroxysteroid dehydrogenase (NAD(+))</skos:prefLabel>
<skos:altLabel>17beta-HSD</skos:altLabel>
<skos:altLabel>17-ketoreductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.239#SIPCF192CDD1DB5201F"/>
<rdfs:comment>Also acts on other 17beta-hydroxysteroids, on the 3alpha-hydroxy group of pregnanes and bile acids.</rdfs:comment>
<rdfs:comment>Different from EC 1.1.1.50 or EC 1.1.1.213.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/2317205"/>
<citation rdf:resource="http://purl.uniprot.org/citations/13696735"/>
<citation rdf:resource="http://purl.uniprot.org/citations/13781425"/>
<citation rdf:resource="http://purl.uniprot.org/citations/15436478"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.239#SIPCF192CDD1DB5201F">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>NAD(+) + testosterone = androst-4-ene-3,17-dione + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/2317205">
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<rdf:Description rdf:about="http://purl.uniprot.org/citations/13696735">
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<rdf:Description rdf:about="http://purl.uniprot.org/citations/13781425">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/13781425"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/13781425"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/15436478">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/15436478"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/15436478"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.240">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>N-acetylhexosamine 1-dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.240#SIP9FFD9B7AC7088C85"/>
<rdfs:comment>Also acts on N-acetylgalactosamine and, more slowly, on N-acetylmannosamine.</rdfs:comment>
<rdfs:comment>Anomeric specificity was tested with N-acetyl-D-glucosamine, and it was shown that the enzyme is specific for the alpha anomer.</rdfs:comment>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.240#SIP9FFD9B7AC7088C85">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>H2O + N-acetyl-alpha-D-glucosamine + NAD(+) = 2 H(+) + N-acetyl-D-glucosaminate + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.241">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>6-endo-hydroxycineole dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.241#SIP6ECBD4E589A12916"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.241#SIP6ECBD4E589A12916">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>2-exo-hydroxy-1,8-cineole + NAD(+) = 6-oxocineole + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.242">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<obsolete rdf:datatype="http://www.w3.org/2001/XMLSchema#boolean">true</obsolete>
<replacedBy rdf:resource="http://purl.uniprot.org/enzyme/1.3.1.69"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.243">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>carveol dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.243#SIP8F347E3760214185"/>
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<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.243#SIP8F347E3760214185">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(1S,5R)-carveol + NADP(+) = (R)-carvone + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/16666709">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.244">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>methanol dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.244#SIPF36524CCCA444535"/>
<citation rdf:resource="http://purl.uniprot.org/citations/2673121"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.244#SIPF36524CCCA444535">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>methanol + NAD(+) = formaldehyde + H(+) + NADH.</rdfs:label>
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<rdfs:comment>Also oxidizes some other alicyclic alcohols and diols.</rdfs:comment>
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<rdfs:label>cyclohexanol + NAD(+) = cyclohexanone + H(+) + NADH.</rdfs:label>
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<rdfs:label>codeine + NADP(+) = codeinone + H(+) + NADPH.</rdfs:label>
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<skos:prefLabel>salutaridine reductase (NADPH)</skos:prefLabel>
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<rdfs:comment>Catalyzes the reversible reduction of salutaridine to salutaridinol, which is a direct precursor of morphinan alkaloids in the poppy plant.</rdfs:comment>
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<rdfs:label>(7S)-salutaridinol + NADP(+) = H(+) + NADPH + salutaridine.</rdfs:label>
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<skos:prefLabel>D-arabinitol 2-dehydrogenase</skos:prefLabel>
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<rdfs:label>D-arabinitol + NAD(+) = D-ribulose + H(+) + NADH.</rdfs:label>
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<skos:prefLabel>galactitol-1-phosphate 5-dehydrogenase</skos:prefLabel>
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<rdfs:comment>The enzyme from the bacterium Escherichia coli is involved in a galactitol degradation pathway.</rdfs:comment>
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<rdfs:label>galactitol 1-phosphate + NAD(+) = H(+) + keto-D-tagatose 6-phosphate + NADH.</rdfs:label>
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<rdfs:comment>Reduces 1,3,6,8-tetrahydroxynaphthalene to scytalone and also reduces 1,3,8-trihydroxynaphthalene to vermelone.</rdfs:comment>
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<rdfs:label>NADP(+) + scytalone = H(+) + NADPH + naphthalene-1,3,6,8-tetrol.</rdfs:label>
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<skos:prefLabel>(S)-carnitine 3-dehydrogenase</skos:prefLabel>
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<rdfs:comment>Specific for the (S)-enantiomer of carnitine, i.e., the enantiomer of the substrate of EC 1.1.1.108.</rdfs:comment>
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<rdfs:label>(S)-carnitine + NAD(+) = 3-dehydrocarnitine + H(+) + NADH.</rdfs:label>
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<skos:prefLabel>mannitol dehydrogenase</skos:prefLabel>
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<rdfs:comment>The enzyme from Apium graveolens (celery) oxidizes alditols with a minimum requirement of 2R chirality at the carbon adjacent to the primary carbon undergoing the oxidation.</rdfs:comment>
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<rdfs:label>D-mannitol + NAD(+) = D-mannose + H(+) + NADH.</rdfs:label>
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<skos:prefLabel>fluoren-9-ol dehydrogenase</skos:prefLabel>
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<rdfs:comment>Involved in the pathway for fluorene metabolism in Arthrobacter sp.</rdfs:comment>
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<rdfs:label>9H-fluoren-9-ol + NADP(+) = 9H-fluoren-9-one + H(+) + NADPH.</rdfs:label>
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<rdfs:label>9H-fluoren-9-ol + NAD(+) = 9H-fluoren-9-one + H(+) + NADH.</rdfs:label>
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<skos:prefLabel>4-(hydroxymethyl)benzenesulfonate dehydrogenase</skos:prefLabel>
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<rdfs:comment>Involved in the toluene-4-sulfonate degradation pathway in Comamonas testosteroni.</rdfs:comment>
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<rdfs:label>4-(hydroxymethyl)benzenesulfonate + NAD(+) = 4-formylbenzenesulfonate + H(+) + NADH.</rdfs:label>
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<skos:prefLabel>6-hydroxyhexanoate dehydrogenase</skos:prefLabel>
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<rdfs:comment>Involved in the cyclohexanol degradation pathway in Acinetobacter NCIB 9871.</rdfs:comment>
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<rdfs:label>6-hydroxyhexanoate + NAD(+) = 6-oxohexanoate + H(+) + NADH.</rdfs:label>
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<skos:prefLabel>3-hydroxypimeloyl-CoA dehydrogenase</skos:prefLabel>
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<rdfs:comment>Involved in the anaerobic pathway of benzoate degradation in bacteria.</rdfs:comment>
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<rdfs:label>3-hydroxy-6-carboxyhexanoyl-CoA + NAD(+) = 3-oxo-6-carboxyhexanoyl-CoA + H(+) + NADH.</rdfs:label>
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<skos:prefLabel>sulcatone reductase</skos:prefLabel>
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<rdfs:comment>Studies on the effects of growth-stage and nutrient supply on the stereochemistry of sulcatone reduction in Clostridia pasteurianum, C. tyrobutyricum and Lactobacillus brevis suggest that there may be at least two sulcatone reductases with different stereospecificities.</rdfs:comment>
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<rdfs:label>NAD(+) + sulcatol = H(+) + NADH + sulcatone.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.261">
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<skos:prefLabel>sn-glycerol-1-phosphate dehydrogenase</skos:prefLabel>
<skos:altLabel>glycerol-1-phosphate dehydrogenase [NAD(P)(+)]</skos:altLabel>
<skos:altLabel>Gro1PDH</skos:altLabel>
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<rdfs:comment>Responsible for the formation of archaea-specific sn-glycerol-1-phosphate, the first step in the biosynthesis of polar lipids in archaea.</rdfs:comment>
<rdfs:comment>It is the enantiomer of sn-glycerol 3-phosphate, the form of glycerophosphate found in bacteria and eukaryotes.</rdfs:comment>
<rdfs:comment>The other enzymes involved in the biosynthesis of polar lipids in archaea are EC 2.5.1.41 and EC 2.5.1.42, which together alkylate the hydroxy groups of glycerol 1-phosphate to give unsaturated archaetidic acid, which is acted upon by EC 2.7.7.67 to form CDP-unsaturated archaeol.</rdfs:comment>
<rdfs:comment>The final step in the pathway involves the addition of L-serine, with concomitant removal of CMP, leading to the production of unsaturated archaetidylserine.</rdfs:comment>
<rdfs:comment>Activity of the enzyme is stimulated by K(+).</rdfs:comment>
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<rdfs:label>NAD(+) + sn-glycerol 1-phosphate = dihydroxyacetone phosphate + H(+) + NADH.</rdfs:label>
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<rdfs:label>NADP(+) + sn-glycerol 1-phosphate = dihydroxyacetone phosphate + H(+) + NADPH.</rdfs:label>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>4-hydroxythreonine-4-phosphate dehydrogenase</skos:prefLabel>
<skos:altLabel>4-(phosphohydroxy)-L-threonine dehydrogenase</skos:altLabel>
<skos:altLabel>L-threonine 4-phosphate dehydrogenase</skos:altLabel>
<skos:altLabel>NAD(+)-dependent threonine 4-phosphate dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.262#SIP70FD4C220E4AD2DC"/>
<rdfs:comment>The enzyme is part of the biosynthesis pathway of the coenzyme pyridoxal 5'-phosphate found in anaerobic bacteria.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/10225425"/>
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<rdfs:label>4-(phosphooxy)-L-threonine + NAD(+) = 3-amino-2-oxopropyl phosphate + CO2 + NADH.</rdfs:label>
</rdf:Description>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>1,5-anhydro-D-fructose reductase</skos:prefLabel>
<skos:altLabel>AF reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.263#SIPE6E3A27BD691FE69"/>
<rdfs:comment>Also reduces pyridine-3-aldehyde and 2,3-butanedione.</rdfs:comment>
<rdfs:comment>Acetaldehyde, 2-dehydroglucose (glucosone) and glucuronate are poor substrates, but there is no detectable action on glucose, mannose and fructose.</rdfs:comment>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>1,5-anhydro-D-glucitol + NADP(+) = 1,5-anhydro-D-fructose + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.264">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>L-idonate 5-dehydrogenase [NAD(P)(+)]</skos:prefLabel>
<skos:altLabel>L-idonate 5-dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.264#SIPB6348E50AA0B9168"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.264#SIPF40A51C401AC22FE"/>
<rdfs:comment>The enzyme from the bacterium Escherichia coli is specific for 5-dehydro-D-gluconate.</rdfs:comment>
<rdfs:comment>Cf. EC 1.1.1.366.</rdfs:comment>
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<rdfs:label>L-idonate + NAD(+) = 5-dehydro-D-gluconate + H(+) + NADH.</rdfs:label>
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<rdfs:label>L-idonate + NADP(+) = 5-dehydro-D-gluconate + H(+) + NADPH.</rdfs:label>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.265">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>3-methylbutanal reductase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.265#SIPFFB811FD48FCF025"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.265#SIPDD2DDD0ED6342A3C"/>
<rdfs:comment>The enzyme purified from Saccharomyces cerevisiae catalyzes the reduction of a number of straight-chain and branched aldehydes, as well as some aromatic aldehydes.</rdfs:comment>
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<rdfs:label>3-methylbutanol + NADP(+) = 3-methylbutanal + H(+) + NADPH.</rdfs:label>
</rdf:Description>
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<rdfs:label>3-methylbutanol + NAD(+) = 3-methylbutanal + H(+) + NADH.</rdfs:label>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.266">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>dTDP-4-dehydro-6-deoxyglucose reductase</skos:prefLabel>
<skos:altLabel>dTDP-4-keto-6-deoxyglucose reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.266#SIP191CDEE8A9AD7183"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.266#SIPA8EA1B4417D8A069"/>
<rdfs:comment>The enzymes from the Gram-negative bacteria Actinobacillus actinomycetemcomitans and Escherichia coli O52 are involved in activation of fucose for incorporation into capsular polysaccharide O-antigens.</rdfs:comment>
<rdfs:comment>The enzyme from the Gram-positive bacterium Anoxybacillus tepidamans (Geobacillus tepidamans) is involved in activation of fucose for incorporation into the organism's S-layer.</rdfs:comment>
<rdfs:comment>The enzyme from E. coli O52 has a higher catalytic efficiency with NADH than with NADPH.</rdfs:comment>
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<rdfs:label>dTDP-alpha-D-fucose + NAD(+) = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H(+) + NADH.</rdfs:label>
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<rdfs:label>dTDP-alpha-D-fucose + NADP(+) = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H(+) + NADPH.</rdfs:label>
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<dcterms:identifier>doi:10.1093/glycob/cwl084</dcterms:identifier>
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<dcterms:identifier>doi:10.1111/j.1365-2958.2008.06449.x</dcterms:identifier>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.267">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>1-deoxy-D-xylulose-5-phosphate reductoisomerase</skos:prefLabel>
<skos:altLabel>1-deoxyxylulose-5-phosphate reductoisomerase</skos:altLabel>
<skos:altLabel>DXP-reductoisomerase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.267#SIPD85463726E145BF3"/>
<rdfs:comment>The enzyme from several eubacteria, including Escherichia coli, forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis.</rdfs:comment>
<rdfs:comment>The mechanism has been shown to be a retroaldol/aldol reaction.</rdfs:comment>
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<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdfs:label>2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH.</rdfs:label>
</rdf:Description>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>2-(R)-hydroxypropyl-CoM dehydrogenase</skos:prefLabel>
<skos:altLabel>2-(2-(R)-hydroxypropylthio)ethanesulfonate dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.268#SIP770CF64164D1DC81"/>
<rdfs:comment>Highly specific for (R)-2-hydroxyalkyl thioethers of CoM, in contrast to EC 1.1.1.269, which is highly specific for the (S)-enantiomer.</rdfs:comment>
<rdfs:comment>Forms component III of a four-component enzyme system (comprising EC 4.4.1.23 (component I), EC 1.8.1.5 (component II), EC 1.1.1.268 (component III) and EC 1.1.1.269 (component IV)) that is involved in epoxyalkane carboxylation in Xanthobacter sp. strain Py2.</rdfs:comment>
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<rdfs:label>(R)-2-hydroxypropyl-coenzyme M + NAD(+) = 2-oxopropyl-coenzyme M + H(+) + NADH.</rdfs:label>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>2-(S)-hydroxypropyl-CoM dehydrogenase</skos:prefLabel>
<skos:altLabel>2-(2-(S)-hydroxypropylthio)ethanesulfonate dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.269#SIP05CD5850C1CDB585"/>
<rdfs:comment>Highly specific for (S)-2-hydroxyalkyl thioethers of CoM, in contrast to EC 1.1.1.268, which is highly specific for the (R)-enantiomer.</rdfs:comment>
<rdfs:comment>Forms component IV of a four-component enzyme system (comprising EC 4.4.1.23 (component I), EC 1.8.1.5 (component II), EC 1.1.1.268 (component III) and EC 1.1.1.269 (component IV)) that is involved in epoxyalkane carboxylation in Xanthobacter sp. strain Py2.</rdfs:comment>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.269#SIP05CD5850C1CDB585">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(2S)-2-hydroxypropyl-coenzyme M + NAD(+) = 2-oxopropyl-coenzyme M + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.270">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>3beta-hydroxysteroid 3-dehydrogenase</skos:prefLabel>
<skos:altLabel>3-keto-steroid reductase</skos:altLabel>
<skos:altLabel>3-KSR</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.270#SIPF06CF525EF0ECD58"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.270#SIPF5335524D0255971"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.270#SIP97E6E825EC701315"/>
<rdfs:comment>The enzyme acts on multiple 3beta-hydroxysteroids.</rdfs:comment>
<rdfs:comment>Participates in the biosynthesis of zemosterol and cholesterol, where it catalyzes the reaction in the opposite direction to that shown.</rdfs:comment>
<rdfs:comment>The mammalian enzyme is bifunctional and also catalyzes EC 1.1.1.62.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/4387005"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.270#SIPF06CF525EF0ECD58">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>a 3beta-hydroxysteroid + NADP(+) = a 3-oxosteroid + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.270#SIPF5335524D0255971">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>4alpha-methyl-5alpha-cholest-7-en-3beta-ol + NADP(+) = 4alpha-methyl-5alpha-cholest-7-en-3-one + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.270#SIP97E6E825EC701315">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>3-dehydro-4alpha-methylzymosterol + H(+) + NADPH = 4alpha-methylzymosterol + NADP(+).</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.271">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>GDP-L-fucose synthase</skos:prefLabel>
<skos:altLabel>GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase</skos:altLabel>
<skos:altLabel>GDP-fucose synthetase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.271#SIPEAFA2EC4CEAD9920"/>
<rdfs:comment>Both human and Escherichia coli enzymes can use NADH in place of NADPH to a slight extent.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/3338988"/>
<citation rdf:resource="http://purl.uniprot.org/citations/9862812"/>
<citation rdf:resource="http://purl.uniprot.org/citations/10480878"/>
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<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.271#SIPEAFA2EC4CEAD9920">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>GDP-beta-L-fucose + NADP(+) = GDP-4-dehydro-alpha-D-rhamnose + H(+) + NADPH.</rdfs:label>
</rdf:Description>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/10480878">
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<rdf:Description rdf:about="http://purl.uniprot.org/citations/11030750">
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.272">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>D-2-hydroxyacid dehydrogenase (NADP(+))</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.272#SIP037347D2B4D9CD37"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.272#SIP142C2E1EF35653C9"/>
<rdfs:comment>This enzyme, characterized from the halophilic archaeon Haloferax mediterranei and the mold Aspergillus oryzae, catalyzes a reversible stereospecific reduction of 2-oxocarboxylic acids into the corresponding D-2-hydroxycarboxylic acids.</rdfs:comment>
<rdfs:comment>The enzyme prefers substrates with a main chain of 5 carbons (such as 4-methyl-2-oxopentanoate) to those with a shorter chain, and can use NADH with much lower efficiency.</rdfs:comment>
<rdfs:comment>cf. EC 1.1.1.345.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/17049749"/>
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<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.272#SIP037347D2B4D9CD37">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>a (2R)-2-hydroxycarboxylate + NADP(+) = a 2-oxocarboxylate + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.272#SIP142C2E1EF35653C9">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(R)-2-hydroxy-4-methylpentanoate + NADP(+) = 4-methyl-2-oxopentanoate + H(+) + NADPH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.273">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>vellosimine dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.273#SIPA44B80E3B8DAC67B"/>
<rdfs:comment>Also acts on related alkaloids with an endo-aldehyde group such as vellosimine (same stereochemistry at C-16) but only slight activity with exo-aldehydes (epimeric at C-16).</rdfs:comment>
<rdfs:comment>Detected in many cell suspension cultures of plants from the family Apocynaceae.</rdfs:comment>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.273#SIPA44B80E3B8DAC67B">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>10-deoxysarpagine + NADP(+) = H(+) + NADPH + vellosimine.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.274">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming)</skos:prefLabel>
<skos:altLabel>2,5-diketo-D-gluconate reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.274#SIPC497BF1D559A1974"/>
<rdfs:comment>The enzyme is involved in the catabolism of 2,5-didehydrogluconate.</rdfs:comment>
<rdfs:comment>cf. EC 1.1.1.346.</rdfs:comment>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.274#SIPC497BF1D559A1974">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>2-dehydro-D-gluconate + NADP(+) = 2,5-didehydro-D-gluconate + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.275">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>(+)-trans-carveol dehydrogenase</skos:prefLabel>
<skos:altLabel>carveol dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.275#SIPC383EDE67B994D65"/>
<rdfs:comment>NADP(+) cannot replace NAD(+).</rdfs:comment>
<rdfs:comment>Forms part of the monoterpenoid biosynthesis pathway in Carum carvi (caraway) seeds.</rdfs:comment>
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<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.275#SIPC383EDE67B994D65">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(1R,5S)-carveol + NAD(+) = (S)-carvone + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.276">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>serine 3-dehydrogenase (NADP(+))</skos:prefLabel>
<skos:altLabel>serine 3-dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.276#SIP9DB53F65F0604EEE"/>
<rdfs:comment>NAD(+) cannot replace NADP(+) (cf. EC 1.1.1.387).</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/9028042"/>
<citation rdf:resource="http://purl.uniprot.org/citations/12092831"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.276#SIP9DB53F65F0604EEE">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>L-serine + NADP(+) = aminoacetaldehyde + CO2 + NADPH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.277">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>3beta-hydroxy-5beta-steroid dehydrogenase</skos:prefLabel>
<skos:altLabel>3beta-hydroxysteroid 5beta-oxidoreductase</skos:altLabel>
<skos:altLabel>3beta-hydroxysteroid 5beta-progesterone oxidoreductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.277#SIP9E88B67924C41F5A"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.277#SIP9E88B67924C41F5A">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>3beta-hydroxy-5beta-pregnane-20-one + NADP(+) = 5beta-pregnan-3,20-dione + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.278">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>3beta-hydroxy-5alpha-steroid dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.278#SIPF97A39611758A5F4"/>
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<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.278#SIPF97A39611758A5F4">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>3beta-hydroxy-5alpha-pregnane-20-one + NADP(+) = 5alpha-pregnane-3,20-dione + H(+) + NADPH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.279">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<replaces rdf:resource="http://purl.uniprot.org/enzyme/1.2.1.55"/>
<skos:prefLabel>(R)-3-hydroxyacid-ester dehydrogenase</skos:prefLabel>
<skos:altLabel>3-oxo ester (R)-reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.279#SIP6D62472CCE5B3369"/>
<rdfs:comment>Also acts on ethyl (R)-3-oxobutanoate and some other (R)-3-hydroxy acid esters.</rdfs:comment>
<rdfs:comment>The (R)- symbol is allotted on the assumption that no substituents change the order of priority from O-3>C-2>C-4.</rdfs:comment>
<rdfs:comment>A subunit of Saccharomyces cerevisiae EC 2.3.1.86.</rdfs:comment>
<rdfs:comment>Cf. EC 1.1.1.280.</rdfs:comment>
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<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.279#SIP6D62472CCE5B3369">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>ethyl (R)-3-hydroxyhexanoate + NADP(+) = ethyl 3-oxohexanoate + H(+) + NADPH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.280">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<replaces rdf:resource="http://purl.uniprot.org/enzyme/1.2.1.56"/>
<skos:prefLabel>(S)-3-hydroxyacid-ester dehydrogenase</skos:prefLabel>
<skos:altLabel>3-oxo ester (S)-reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.280#SIPC57AB737A352E78A"/>
<rdfs:comment>Also acts on 4-oxo- and 5-oxo-fatty acids and their esters.</rdfs:comment>
<rdfs:comment>Cf. EC 1.1.1.279.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/3280313"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.280#SIPC57AB737A352E78A">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>ethyl (S)-3-hydroxyhexanoate + NADP(+) = ethyl 3-oxohexanoate + H(+) + NADPH.</rdfs:label>
</rdf:Description>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.281">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>GDP-4-dehydro-6-deoxy-D-mannose reductase</skos:prefLabel>
<skos:altLabel>GDP-4-keto-6-deoxy-D-mannose reductase</skos:altLabel>
<skos:altLabel>GDP-6-deoxy-D-lyxo-4-hexulose reductase</skos:altLabel>
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<rdfs:comment>Differs from EC 1.1.1.187 in that the only product formed is GDP-alpha-D-rhamnose (GDP-6-deoxy-alpha-D-mannose).</rdfs:comment>
<rdfs:comment>D-rhamnose is a constituent of lipopolysaccharides of Gram-negative plant and human pathogenic bacteria.</rdfs:comment>
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<rdfs:label>GDP-alpha-D-rhamnose + NAD(+) = GDP-4-dehydro-alpha-D-rhamnose + H(+) + NADH.</rdfs:label>
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<rdfs:label>GDP-alpha-D-rhamnose + NADP(+) = GDP-4-dehydro-alpha-D-rhamnose + H(+) + NADPH.</rdfs:label>
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<skos:prefLabel>quinate/shikimate dehydrogenase [NAD(P)(+)]</skos:prefLabel>
<skos:altLabel>quinate/shikimate dehydrogenase</skos:altLabel>
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<rdfs:comment>This is the second shikimate dehydrogenase enzyme found in Escherichia coli.</rdfs:comment>
<rdfs:comment>It can use both quinate and shikimate as substrates and either NAD(+) or NADP(+) as acceptor.</rdfs:comment>
<rdfs:comment>The low catalytic efficiency with both quinate and shikimate suggests that neither may be the physiological substrate.</rdfs:comment>
<rdfs:comment>Cf. EC 1.1.1.24, EC 1.1.1.25, and EC 1.1.5.8.</rdfs:comment>
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<rdfs:label>L-quinate + NADP(+) = 3-dehydroquinate + H(+) + NADPH.</rdfs:label>
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<rdfs:label>L-quinate + NAD(+) = 3-dehydroquinate + H(+) + NADH.</rdfs:label>
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<rdfs:label>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH.</rdfs:label>
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<rdfs:label>NAD(+) + shikimate = 3-dehydroshikimate + H(+) + NADH.</rdfs:label>
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<skos:prefLabel>methylglyoxal reductase (NADPH)</skos:prefLabel>
<skos:altLabel>lactaldehyde dehydrogenase (NADP(+))</skos:altLabel>
<skos:altLabel>methylglyoxal reductase (NADPH-dependent)</skos:altLabel>
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<rdfs:comment>The enzyme from the yeast Saccharomyces cerevisiae catalyzes the reduction of a keto group in a number of compounds, forming enantiopure products.</rdfs:comment>
<rdfs:comment>Among the substrates are methylglyoxal (which is reduced to (S)-lactaldehyde), 3-methylbutanal, hexane-2,5-dione and 3-chloro-1-phenylpropan-1-one.</rdfs:comment>
<rdfs:comment>The enzyme differs from EC 1.1.1.78 which is found in mammals, by its coenzyme requirement, reaction direction, and enantiomeric preference.</rdfs:comment>
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<rdfs:label>(S)-lactaldehyde + NADP(+) = H(+) + methylglyoxal + NADPH.</rdfs:label>
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<skos:prefLabel>S-(hydroxymethyl)glutathione dehydrogenase</skos:prefLabel>
<skos:altLabel>ADH3</skos:altLabel>
<skos:altLabel>chi-ADH</skos:altLabel>
<skos:altLabel>class III alcohol dehydrogenase</skos:altLabel>
<skos:altLabel>FDH</skos:altLabel>
<skos:altLabel>formaldehyde dehydrogenase</skos:altLabel>
<skos:altLabel>formaldehyde dehydrogenase (glutathione)</skos:altLabel>
<skos:altLabel>formic dehydrogenase</skos:altLabel>
<skos:altLabel>GD-FALDH</skos:altLabel>
<skos:altLabel>glutathione-dependent formaldehyde dehydrogenase</skos:altLabel>
<skos:altLabel>GS-FDH</skos:altLabel>
<skos:altLabel>NAD- and glutathione-dependent formaldehyde dehydrogenase</skos:altLabel>
<skos:altLabel>NAD-dependent formaldehyde dehydrogenase</skos:altLabel>
<skos:altLabel>NAD-linked formaldehyde dehydrogenase</skos:altLabel>
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<rdfs:comment>The substrate, S-(hydroxymethyl)glutathione, forms spontaneously from glutathione and formaldehyde; its rate of formation is increased in some bacteria by the presence of EC 4.4.1.22.</rdfs:comment>
<rdfs:comment>Forms part of the pathway that detoxifies formaldehyde, since the product is hydrolyzed by EC 3.1.2.12.</rdfs:comment>
<rdfs:comment>Also specifically reduces S-nitrosylglutathione.</rdfs:comment>
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<rdfs:label>NADP(+) + S-(hydroxymethyl)glutathione = H(+) + NADPH + S-formylglutathione.</rdfs:label>
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<rdfs:label>NAD(+) + S-(hydroxymethyl)glutathione = H(+) + NADH + S-formylglutathione.</rdfs:label>
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<skos:prefLabel>3''-deamino-3''-oxonicotianamine reductase</skos:prefLabel>
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<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.285#SIPB0FF2A7266ED9A7E"/>
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<rdfs:label>2'-deoxymugineate + NADP(+) = 3''-deamino-3''-oxonicotianamine + H(+) + NADPH.</rdfs:label>
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<rdfs:label>2'-deoxymugineate + NAD(+) = 3''-deamino-3''-oxonicotianamine + H(+) + NADH.</rdfs:label>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>isocitrate--homoisocitrate dehydrogenase</skos:prefLabel>
<skos:altLabel>homoisocitrate--isocitrate dehydrogenase</skos:altLabel>
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<rdfs:comment>Unlike EC 1.1.1.41 and EC 1.1.1.87, this enzyme, from Pyrococcus horikoshii, can use both isocitrate and homoisocitrate as substrate.</rdfs:comment>
<rdfs:comment>May play a role in both the lysine and glutamate biosynthesis pathways.</rdfs:comment>
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<rdfs:label>D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH.</rdfs:label>
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<rdfs:label>(2R,3S)-homoisocitrate + NAD(+) = 2-oxoadipate + CO2 + NADH.</rdfs:label>
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<skos:prefLabel>D-arabinitol dehydrogenase (NADP(+))</skos:prefLabel>
<skos:altLabel>D-arabinitol dehydrogenase 1</skos:altLabel>
<skos:altLabel>NADP(+)-dependent D-arabinitol dehydrogenase</skos:altLabel>
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<rdfs:comment>The enzyme from the rust fungus Uromyces fabae can use D-arabinitol and D-mannitol as substrates in the forward direction and D-xylulose, D-ribulose and, to a lesser extent, D-fructose as substrates in the reverse direction.</rdfs:comment>
<rdfs:comment>This enzyme carries out the reactions of both EC 1.1.1.11 and EC 1.1.1.250, but unlike them, uses NADP(+) rather than NAD(+) as cofactor.</rdfs:comment>
<rdfs:comment>D-Arabinitol is capable of quenching reactive oxygen species involved in defense reactions of the host plant.</rdfs:comment>
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<rdfs:label>D-arabinitol + NADP(+) = D-xylulose + H(+) + NADPH.</rdfs:label>
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<rdfs:label>D-arabinitol + NADP(+) = D-ribulose + H(+) + NADPH.</rdfs:label>
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<skos:prefLabel>xanthoxin dehydrogenase</skos:prefLabel>
<skos:altLabel>xanthoxin oxidase</skos:altLabel>
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<rdfs:comment>NADP(+) cannot replace NAD(+) and short-chain alcohols such as ethanol, isopropanol, butanol and cyclohexanol cannot replace xanthoxin as substrate.</rdfs:comment>
<rdfs:comment>Involved in the abscisic-acid biosynthesis pathway in plants, along with EC 1.2.3.14, EC 1.13.11.51 and EC 1.14.13.93.</rdfs:comment>
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<rdfs:label>2-cis,4-trans-xanthoxin + NAD(+) = 2-cis-(+)-abscisic aldehyde + H(+) + NADH.</rdfs:label>
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<skos:prefLabel>sorbose reductase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.289#SIPB1C2E481C1ECE0E9"/>
<rdfs:comment>The reaction occurs predominantly in the reverse direction.</rdfs:comment>
<rdfs:comment>This enzyme can also convert D-fructose into D-mannitol, but more slowly.</rdfs:comment>
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<rdfs:label>D-sorbitol + NADP(+) = H(+) + keto-L-sorbose + NADPH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.290">
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<skos:prefLabel>4-phosphoerythronate dehydrogenase</skos:prefLabel>
<skos:altLabel>4-O-phosphoerythronate dehydrogenase</skos:altLabel>
<skos:altLabel>4PE dehydrogenase</skos:altLabel>
<skos:altLabel>erythronate-4-phosphate dehydrogenase</skos:altLabel>
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<rdfs:comment>This enzyme catalyzes a step in a bacterial pathway for the biosynthesis of pyridoxal 5'-phosphate.</rdfs:comment>
<rdfs:comment>The enzyme contains a tightly-bound NAD(H) cofactor that is not re-oxidized by free NAD(+).</rdfs:comment>
<rdfs:comment>In order to re-oxidize the cofactor and restore enzyme activity, the enzyme catalyzes the reduction of a 2-oxo acid (such as 2-oxoglutarate, oxaloacetate, or pyruvate) to the respective (R)-hydroxy acid.</rdfs:comment>
<rdfs:comment>Cf. EC 1.1.1.399.</rdfs:comment>
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<rdfs:label>4-phospho-D-erythronate + NAD(+) = (R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + H(+) + NADH.</rdfs:label>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.291">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>2-hydroxymethylglutarate dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.291#SIP6F3B6DE52C0883F4"/>
<rdfs:comment>NADP(+) cannot replace NAD(+).</rdfs:comment>
<rdfs:comment>Forms part of the nicotinate-fermentation catabolism pathway in Eubacterium barkeri.</rdfs:comment>
<rdfs:comment>Other enzymes involved in this pathway are EC 1.17.1.5, EC 1.3.7.1, EC 3.5.2.18, EC 5.4.99.4, EC 5.3.3.6, EC 4.2.1.85 and EC 4.1.3.32.</rdfs:comment>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.291#SIP6F3B6DE52C0883F4">
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<rdfs:label>(S)-2-hydroxymethylglutarate + NAD(+) = 2-formylglutarate + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.292">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming)</skos:prefLabel>
<skos:altLabel>1,5-anhydro-D-fructose reductase</skos:altLabel>
<skos:altLabel>AFR</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.292#SIPCE4E81FABD91BD59"/>
<rdfs:comment>Present in some but not all Rhizobium species.</rdfs:comment>
<rdfs:comment>Differs from hepatic 1,5-anhydro-D-fructose reductase, which yields 1,5-anhydro-D-glucitol as the product (see EC 1.1.1.263).</rdfs:comment>
<rdfs:comment>In Sinorhizobium morelense, the product of the reaction, 1,5-anhydro-D-mannitol, can be further metabolized to D-mannose.</rdfs:comment>
<rdfs:comment>Also reduces 1,5-anhydro-D-erythro-hexo-2,3-diulose and 2-ketoaldoses (called osones), such as D-glucosone (D-arabino-hexos-2-ulose) and 6-deoxy-D-glucosone.</rdfs:comment>
<rdfs:comment>Does not reduce common aldoses and ketoses, or non-sugar aldehydes and ketones.</rdfs:comment>
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<rdfs:label>1,5-anhydro-D-mannitol + NADP(+) = 1,5-anhydro-D-fructose + H(+) + NADPH.</rdfs:label>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.293">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<obsolete rdf:datatype="http://www.w3.org/2001/XMLSchema#boolean">true</obsolete>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.294">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>chlorophyll(ide) b reductase</skos:prefLabel>
<skos:altLabel>Chl b reductase</skos:altLabel>
<skos:altLabel>chlorophyll b reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.294#SIP328CA90D8DC1CFDE"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.294#SIP7C61188225518DF7"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.294#SIPA4FBD95062ED180F"/>
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<rdfs:comment>Carries out the first step in the conversion of chlorophyll b to chlorophyll a.</rdfs:comment>
<rdfs:comment>Involved in chlorophyll degradation, which occurs during leaf senescence and it also forms part of the chlorophyll cycle, which interconverts chlorophyll a and b in response to changing light conditions.</rdfs:comment>
<rdfs:comment>While both chlorophyll a and chlorophyll b are found in higher plants, only breakdown products derived from chlorophyll a are found in the end products, i.e. non-fluorescent chlorophyll catabolites (NCCs).</rdfs:comment>
<rdfs:comment>The transition from chlorophyll b, which contains a formyl group on C7, to chlorophyll a, which contains a methyl group on C7, proceeds through the intermediate 7(1)-hydroxychlorophyll.</rdfs:comment>
<rdfs:comment>Another enzyme, which requires ferredoxin but has not been characterized fully, is required to complete the conversion.</rdfs:comment>
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<rdfs:label>7(1)-hydroxychlorophyllide a + NAD(+) = chlorophyllide b + H(+) + NADH.</rdfs:label>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.294#SIP7C61188225518DF7">
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<rdfs:label>7(1)-hydroxychlorophyllide a + NADP(+) = chlorophyllide b + H(+) + NADPH.</rdfs:label>
</rdf:Description>
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<rdfs:label>7(1)-hydroxychlorophyll a + NAD(+) = chlorophyll b + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdfs:label>7(1)-hydroxychlorophyll a + NADP(+) = chlorophyll b + H(+) + NADPH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.295">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>momilactone-A synthase</skos:prefLabel>
<skos:altLabel>momilactone A synthase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.295#SIPF793186EC3D6E40C"/>
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<rdfs:comment>The rice phytoalexin momilactone A is a diterpenoid secondary metabolite that is involved in the defense mechanism of the plant.</rdfs:comment>
<rdfs:comment>Momilactone A is produced in response to attack by a pathogen through the perception of elicitor signal molecules such as chitin oligosaccharide, or after exposure to UV irradiation.</rdfs:comment>
<rdfs:comment>The enzyme, which catalyzes the last step in the biosynthesis of momilactone A, can use both NAD(+) and NADP(+) but activity is higher with NAD(+).</rdfs:comment>
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<rdfs:label>3beta-hydroxy-9beta-pimara-7,15-dien-19,6beta-olide + NAD(+) = H(+) + momilactone A + NADH.</rdfs:label>
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<rdfs:label>3beta-hydroxy-9beta-pimara-7,15-dien-19,6beta-olide + NADP(+) = H(+) + momilactone A + NADPH.</rdfs:label>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>dihydrocarveol dehydrogenase</skos:prefLabel>
<skos:altLabel>carveol dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.296#SIP31FA5CF3CB35E559"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.296#SIPCA3CEEB15AFC1447"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.296#SIP0A8CBEDDAF1A1EBF"/>
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<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.296#SIP8EA525D7DEC10A77"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.296#SIPE553D82A51940FC5"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.296#SIP5CDFA9079C7BE40A"/>
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<rdfs:comment>This enzyme from the Gram-positive bacterium Rhodococcus erythropolis DCL14 forms part of the carveol and dihydrocarveol degradation pathway.</rdfs:comment>
<rdfs:comment>Accepts all eight stereoisomers of menth-8-en-2-ol as substrate, although some isomers are converted faster than others.</rdfs:comment>
<rdfs:comment>The preferred substrates are (+)-neoisodihydrocarveol, (+)-isodihydrocarveol, (+)-dihydrocarveol and (-)-isodihydrocarveol.</rdfs:comment>
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<rdfs:label>dihydrocarveol + NAD(+) = dihydrocarvone + H(+) + NADH.</rdfs:label>
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<rdfs:label>(1R,2R,4R)-dihydrocarveol + NAD(+) = (1R,4R)-dihydrocarvone + H(+) + NADH.</rdfs:label>
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<rdfs:label>(1S,2S,4S)-dihydrocarveol + NAD(+) = (1S,4S)-dihydrocarvone + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdfs:label>(1S,2R,4S)-neodihydrocarveol + NAD(+) = (1S,4S)-dihydrocarvone + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdfs:label>(1R,2S,4R)-neodihydrocarveol + NAD(+) = (1R,4R)-dihydrocarvone + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdfs:label>(1R,2S,4S)-neoisodihydrocarveol + NAD(+) = (1R,4S)-isodihydrocarvone + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.296#SIP5CDFA9079C7BE40A">
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<rdfs:label>(1R,2R,4S)-isodihydrocarveol + NAD(+) = (1R,4S)-isodihydrocarvone + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.296#SIP25F95BAD9A080604">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(1S,2S,4R)-isodihydrocarveol + NAD(+) = (1S,4R)-isodihydrocarvone + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.296#SIPFEA470E8B6DB62FE">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(1S,2R,4R)-neoisodihydrocarveol + NAD(+) = (1S,4R)-isodihydrocarvone + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.297">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>limonene-1,2-diol dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.297#SIP4847803941B0C582"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.297#SIPE0B284E25EF52DB1"/>
<rdfs:comment>While the enzyme from the Gram-positive bacterium Rhodococcus erythropolis DCL14 can use both (1S,2S,4R)- and (1R,2R,4S)-menth-8-ene-1,2-diol as substrate, activity is higher with (1S,2S,4R)-menth-8-ene-1,2-diol as substrate.</rdfs:comment>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.297#SIP4847803941B0C582">
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<rdfs:label>(1R,2R,4S)-limonene-1,2-diol + NAD(+) = (1R,4S)-1-hydroxylimonen-2-one + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.297#SIPE0B284E25EF52DB1">
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<rdfs:label>(1S,2S,4R)-limonene-1,2-diol + NAD(+) = (1S,4R)-1-hydroxylimonen-2-one + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.298">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>3-hydroxypropionate dehydrogenase (NADP(+))</skos:prefLabel>
<skos:altLabel>3-hydroxypropanoate dehydrogenase (NADP(+))</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.298#SIPDCA1DEDF56B8EB5B"/>
<rdfs:comment>Catalyzes the reduction of 3-oxopropanoate to 3-hydroxypropanoate, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutyrate cycles, autotrophic CO2 fixation pathways found in some green non-sulfur phototrophic bacteria and archaea, respectively.</rdfs:comment>
<rdfs:comment>The enzyme from Chloroflexus aurantiacus is bifunctional, and also catalyzes the upstream reaction in the pathway, EC 1.2.1.75.</rdfs:comment>
<rdfs:comment>Different from EC 1.1.1.59 by cofactor preference.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/8354269"/>
<citation rdf:resource="http://purl.uniprot.org/citations/11948153"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.298#SIPDCA1DEDF56B8EB5B">
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<rdfs:label>3-hydroxypropanoate + NADP(+) = 3-oxopropanoate + H(+) + NADPH.</rdfs:label>
</rdf:Description>
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<dcterms:identifier>doi:10.1126/science.1149976</dcterms:identifier>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.299">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>malate dehydrogenase [NAD(P)(+)]</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.299#SIPEAE329487AE5C470"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.299#SIP457A2546483EB7EE"/>
<rdfs:comment>This enzyme, which was characterized from the methanogenic archaeon Methanobacterium thermoautotrophicum, catalyzes only the reduction of oxaloacetate, and can use NAD(+) and NADP(+) with similar specific activity.</rdfs:comment>
<rdfs:comment>Different from EC 1.1.1.37, EC 1.1.1.82 and EC 1.1.5.4.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/9639601"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.299#SIPEAE329487AE5C470">
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<rdfs:label>(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.299#SIP457A2546483EB7EE">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(S)-malate + NADP(+) = H(+) + NADPH + oxaloacetate.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.300">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<replaces rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.n2"/>
<skos:prefLabel>NADP-retinol dehydrogenase</skos:prefLabel>
<skos:altLabel>all-trans retinal reductase</skos:altLabel>
<skos:altLabel>all-trans-retinol dehydrogenase</skos:altLabel>
<skos:altLabel>NADP(H)-dependent retinol dehydrogenase/reductase</skos:altLabel>
<skos:altLabel>retinol dehydrogenase [NADP(+)]</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.300#SIPA28954356E241532"/>
<rdfs:comment>Greater catalytic efficiency in the reductive direction.</rdfs:comment>
<rdfs:comment>This observation, and the enzyme's localization at the entrance to the mitochondrial matrix, suggest that it may function to protect mitochondria against oxidative stress associated with the highly reactive retinal produced from dietary beta-carotene by EC 1.13.11.63.</rdfs:comment>
<rdfs:comment>Km-values for NADP(+) and NADPH are at least 800-fold lower than those for NAD(+) and NADH.</rdfs:comment>
<rdfs:comment>This enzyme differs from EC 1.1.1.105 which prefers NAD(+) and NADH.</rdfs:comment>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>all-trans-retinol + NADP(+) = all-trans-retinal + H(+) + NADPH.</rdfs:label>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.301">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<replaces rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.n10"/>
<skos:prefLabel>D-arabitol-phosphate dehydrogenase</skos:prefLabel>
<skos:altLabel>APDH</skos:altLabel>
<skos:altLabel>D-arabitol 1-phosphate dehydrogenase</skos:altLabel>
<skos:altLabel>D-arabitol 5-phosphate dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.301#SIPE55AB6B7E843FB8D"/>
<rdfs:comment>This enzyme participates in arabinitol catabolism.</rdfs:comment>
<rdfs:comment>The enzyme also converts D-arabinitol 5-phosphate to D-ribulose 5-phosphate at a lower rate.</rdfs:comment>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.301#SIPE55AB6B7E843FB8D">
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<rdfs:label>D-arabinitol 1-phosphate + NAD(+) = D-xylulose 5-phosphate + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.302">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>2,5-diamino-6-(ribosylamino)-4(3H)-pyrimidinone 5'-phosphate reductase</skos:prefLabel>
<skos:altLabel>2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.302#SIP0A10EA64255CA228"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.302#SIP5617539A683CFAEF"/>
<rdfs:comment>The reaction proceeds in the opposite direction.</rdfs:comment>
<rdfs:comment>A step in riboflavin biosynthesis, NADPH and NADH function equally well as reductant.</rdfs:comment>
<rdfs:comment>Differs from EC 1.1.1.193 since it does not catalyze the reduction of 5-amino-6-ribosylaminopyrimidine-2,4(1H,3H)-dione 5'-phosphate.</rdfs:comment>
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<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.302#SIP0A10EA64255CA228">
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<rdfs:label>2,5-diamino-6-(1-D-ribitylamino)pyrimidin-4(3H)-one 5'-phosphate + NAD(+) = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.302#SIP5617539A683CFAEF">
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<rdfs:label>2,5-diamino-6-(1-D-ribitylamino)pyrimidin-4(3H)-one 5'-phosphate + NADP(+) = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + H(+) + NADPH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.303">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<replaces rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.5"/>
<skos:prefLabel>diacetyl reductase [(R)-acetoin forming]</skos:prefLabel>
<skos:altLabel>(R)-acetoin dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.303#SIP93C1EE954E8334C2"/>
<rdfs:comment>The reaction is catalyzed in the reverse direction.</rdfs:comment>
<rdfs:comment>This activity is usually associated with butanediol dehydrogenase activity (EC 1.1.1.4 or EC 1.1.1.76).</rdfs:comment>
<rdfs:comment>While the butanediol dehydrogenase activity is reversible, diacetyl reductase activity is irreversible.</rdfs:comment>
<rdfs:comment>This enzyme has been reported in the yeast Saccharomyces cerevisiae.</rdfs:comment>
<rdfs:comment>Different from EC 1.1.1.304.</rdfs:comment>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.303#SIP93C1EE954E8334C2">
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<rdfs:label>(R)-acetoin + NAD(+) = diacetyl + H(+) + NADH.</rdfs:label>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.304">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<replaces rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.5"/>
<skos:prefLabel>diacetyl reductase [(S)-acetoin forming]</skos:prefLabel>
<skos:altLabel>(S)-acetoin dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.304#SIP8DA3395008886A93"/>
<rdfs:comment>The reaction is catalyzed in the reverse direction.</rdfs:comment>
<rdfs:comment>This activity is usually associated with butanediol dehydrogenase activity (EC 1.1.1.4 or EC 1.1.1.76).</rdfs:comment>
<rdfs:comment>While the butanediol dehydrogenase activity is reversible, diacetyl reductase activity is irreversible.</rdfs:comment>
<rdfs:comment>This enzyme has been reported in the bacteria Geobacillus stearothermophilus, Enterobacter aerogenes and Klebsiella pneumoniae.</rdfs:comment>
<rdfs:comment>Different from EC 1.1.1.303.</rdfs:comment>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.304#SIP8DA3395008886A93">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(S)-acetoin + NAD(+) = diacetyl + H(+) + NADH.</rdfs:label>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.305">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<replaces rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.n1"/>
<skos:prefLabel>UDP-glucuronic acid oxidase (UDP-4-keto-hexauronic acid decarboxylating)</skos:prefLabel>
<skos:altLabel>ArnADH</skos:altLabel>
<skos:altLabel>UDP-GlcUA decarboxylase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.305#SIP9F52DD5AE4F4685C"/>
<rdfs:comment>The activity is part of a bifunctional enzyme also performing the reaction of EC 2.1.2.13.</rdfs:comment>
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<rdfs:label>NAD(+) + UDP-alpha-D-glucuronate = CO2 + NADH + UDP-beta-L-threo-pentopyranos-4-ulose.</rdfs:label>
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<skos:prefLabel>S-(hydroxymethyl)mycothiol dehydrogenase</skos:prefLabel>
<skos:altLabel>mycothiol-dependent formaldehyde dehydrogenase</skos:altLabel>
<skos:altLabel>NAD/factor-dependent formaldehyde dehydrogenase</skos:altLabel>
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<rdfs:comment>S-hydroxymethylmycothiol is believed to form spontaneously from formaldehyde and mycothiol.</rdfs:comment>
<rdfs:comment>This enzyme oxidizes the product of this spontaneous reaction to S-formylmycothiol, in a reaction that is analogous to EC 1.1.1.284, S-(hydroxymethyl)glutathione dehydrogenase.</rdfs:comment>
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<rdfs:label>NAD(+) + S-(hydroxymethyl)mycothiol = H(+) + NADH + S-formylmycothiol.</rdfs:label>
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<skos:prefLabel>D-xylose reductase [NAD(P)H]</skos:prefLabel>
<skos:altLabel>D-xylose reductase</skos:altLabel>
<skos:altLabel>xylose reductase</skos:altLabel>
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<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.307#SIP8077DAB55E7C0756"/>
<rdfs:comment>Xylose reductases catalyze the reduction of xylose to xylitol, the initial reaction in the fungal D-xylose degradation pathway.</rdfs:comment>
<rdfs:comment>Most of the enzymes exhibit a strict requirement for NADPH (cf. EC 1.1.1.431).</rdfs:comment>
<rdfs:comment>However, a few D-xylose reductases, such as those from Neurospora crassa, Yamadazyma tenuis, Scheffersomyces stipitis, and the thermophilic fungus Chaetomium thermophilum, have dual coenzyme specificity, though they still prefer NADPH to NADH.</rdfs:comment>
<rdfs:comment>Very rarely the enzyme prefers NADH (cf. EC 1.1.1.430).</rdfs:comment>
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<rdfs:label>NAD(+) + xylitol = D-xylose + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdfs:label>NADP(+) + xylitol = D-xylose + H(+) + NADPH.</rdfs:label>
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<dcterms:identifier>doi:10.1515/bc.1999.179</dcterms:identifier>
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<dcterms:identifier>doi:10.1046/j.1432-1033.2003.03496.x</dcterms:identifier>
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<dcterms:identifier>doi:10.1128/aem.71.3.1642-1647.2005</dcterms:identifier>
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<dcterms:identifier>doi:10.1007/s12038-009-0102-7</dcterms:identifier>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.308">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>sulfopropanediol 3-dehydrogenase</skos:prefLabel>
<skos:altLabel>dihydroxypropanesulfonate 3-dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.308#SIPA5D5B5F4C50E8AB7"/>
<rdfs:comment>The enzyme is involved in degradation of (R)-2,3-dihydroxypropanesulfonate.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/20150239"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdfs:label>(2R)-3-sulfopropanediol + H2O + 2 NAD(+) = (2R)-3-sulfolactate + 3 H(+) + 2 NADH.</rdfs:label>
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<skos:prefLabel>phosphonoacetaldehyde reductase (NADH)</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.309#SIPACFEFA700398DBCE"/>
<rdfs:comment>The enzyme from Streptomyces viridochromogenes catalyzes a step in the biosynthesis of phosphinothricin tripeptide, the reduction of phosphonoacetaldehyde to 2-hydroxyethylphosphonate.</rdfs:comment>
<rdfs:comment>The preferred cofactor is NADH, lower activity with NADPH.</rdfs:comment>
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<rdfs:label>2-hydroxyethylphosphonate + NAD(+) = H(+) + NADH + phosphonoacetaldehyde.</rdfs:label>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>(S)-sulfolactate dehydrogenase</skos:prefLabel>
<skos:altLabel>(2S)-3-sulfolactate dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.310#SIP5C793F54A4CFD0E7"/>
<rdfs:comment>This enzyme, isolated from the bacterium Chromohalobacter salexigens DSM 3043, acts only on the (S)-enantiomer of 3-sulfolactate.</rdfs:comment>
<rdfs:comment>Combined with EC 1.1.1.338, it provides a racemase system that converts (2S)-3-sulfolactate to (2R)-3-sulfolactate, which is degraded further by EC 4.4.1.24.</rdfs:comment>
<rdfs:comment>The enzyme is specific for NAD(+).</rdfs:comment>
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<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdfs:label>(2S)-3-sulfolactate + NAD(+) = 3-sulfopyruvate + H(+) + NADH.</rdfs:label>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>(S)-1-phenylethanol dehydrogenase</skos:prefLabel>
<skos:altLabel>PED</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.311#SIPFA8BBC8AF7239D02"/>
<rdfs:comment>The enzyme is involved in degradation of ethylbenzene.</rdfs:comment>
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<rdfs:label>(S)-1-phenylethanol + NAD(+) = acetophenone + H(+) + NADH.</rdfs:label>
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<replaces rdf:resource="http://purl.uniprot.org/enzyme/1.2.1.45"/>
<skos:prefLabel>2-hydroxy-4-carboxymuconate semialdehyde hemiacetal dehydrogenase</skos:prefLabel>
<skos:altLabel>4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.312#SIP22BDCB002C8E91D6"/>
<rdfs:comment>The enzyme does not act on unsubstituted aliphatic or aromatic aldehydes or glucose; NAD(+) can replace NADP(+), but with lower affinity.</rdfs:comment>
<rdfs:comment>The enzyme was initially believed to act on 4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde and produce 4-carboxy-2-hydroxy-cis,cis-muconate.</rdfs:comment>
<rdfs:comment>However, later studies showed that the substrate is the hemiacetal form, and the product is 2-oxo-2H-pyran-4,6-dicarboxylate.</rdfs:comment>
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<rdfs:label>4-carboxy-2-hydroxymuconate semialdehyde hemiacetal + NADP(+) = 2-oxo-2H-pyran-4,6-dicarboxylate + H(+) + NADPH.</rdfs:label>
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<skos:prefLabel>sulfoacetaldehyde reductase (NADPH)</skos:prefLabel>
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<rdfs:comment>Catalyzes the reaction only in the opposite direction.</rdfs:comment>
<rdfs:comment>Involved in taurine degradation.</rdfs:comment>
<rdfs:comment>The bacterium Chromohalobacter salexigens strain DSM 3043 possesses two enzymes that catalyze this reaction, a constitutive enzyme (encoded by isfD2) and an inducible enzyme (encoded by isfD).</rdfs:comment>
<rdfs:comment>The latter is induced by taurine, and is responsible for most of the activity observed in taurine-grown cells. cf. EC 1.1.1.433.</rdfs:comment>
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<rdfs:label>2-hydroxyethane-1-sulfonate + NADP(+) = H(+) + NADPH + sulfoacetaldehyde.</rdfs:label>
</rdf:Description>
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<dcterms:identifier>doi:10.1099/mic.0.036699-0</dcterms:identifier>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.314">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<obsolete rdf:datatype="http://www.w3.org/2001/XMLSchema#boolean">true</obsolete>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.315">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>11-cis-retinol dehydrogenase</skos:prefLabel>
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<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.315#SIP01F8115C3E5E0C47"/>
<rdfs:comment>This enzyme, abundant in the retinal pigment epithelium, catalyzes the reduction of 11-cis-retinol to 11-cis-retinal while the substrate is bound to the retinal-binding protein.</rdfs:comment>
<rdfs:comment>This is a crucial step in the regeneration of 11-cis-retinal, the chromophore of rhodopsin.</rdfs:comment>
<rdfs:comment>The enzyme can also accept other cis forms of retinol.</rdfs:comment>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.315#SIP7F8E9ABA23CF0F9C">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>11-cis-retinol--[retinol-binding protein] + NAD(+) = 11-cis-retinal--[retinol-binding protein] + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.315#SIP01F8115C3E5E0C47">
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<rdfs:label>11-cis-retinol + NAD(+) = 11-cis-retinal + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.316">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>L-galactose 1-dehydrogenase</skos:prefLabel>
<skos:altLabel>L-galactose dehydrogenase</skos:altLabel>
<skos:altLabel>L-GalDH</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.316#SIPEC8BF064699F0173"/>
<rdfs:comment>The enzyme catalyzes a step in the ascorbate biosynthesis in higher plants (Smirnoff-Wheeler pathway).</rdfs:comment>
<rdfs:comment>The activity with NADP(+) is less than 10% of the activity with NAD(+).</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/9620799"/>
<citation rdf:resource="http://purl.uniprot.org/citations/12047629"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.316#SIPEC8BF064699F0173">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>L-galactose + NAD(+) = H(+) + L-galactono-1,4-lactone + NADH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/citations/15509850">
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<rdf:Description rdf:about="http://purl.uniprot.org/citations/19297184">
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<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/19297184"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.317">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>perakine reductase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.317#SIPA739BA7C17AAC6AD"/>
<rdfs:comment>The biosynthesis of raucaffrinoline from perakine is a side route of the ajmaline biosynthesis pathway.</rdfs:comment>
<rdfs:comment>The enzyme is a member of the aldo-keto reductase enzyme superfamily from higher plants.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/17142919"/>
<citation rdf:resource="http://purl.uniprot.org/citations/18409028"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.317#SIPA739BA7C17AAC6AD">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>NADP(+) + raucaffrinoline = H(+) + NADPH + perakine.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/citations/18409028">
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.318">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>eugenol synthase</skos:prefLabel>
<skos:altLabel>EGS2</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.318#SIPC5E4375905480424"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.318#SIPAD9288C2825B6DBB"/>
<rdfs:comment>The enzyme acts in the opposite direction.</rdfs:comment>
<rdfs:comment>The enzymes from the plants Ocimum basilicum (sweet basil), Clarkia breweri and Petunia hybrida only accept coniferyl acetate and form eugenol.</rdfs:comment>
<rdfs:comment>The enzyme from Pimpinella anisum (anise) forms anol (from 4-coumaryl acetate) in vivo, although the recombinant enzyme can form eugenol from coniferyl acetate.</rdfs:comment>
<rdfs:comment>The enzyme from Larrea tridentata (creosote bush) also forms chavicol from a coumaryl ester and can use NADH.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/16782809"/>
<citation rdf:resource="http://purl.uniprot.org/citations/17624297"/>
<citation rdf:resource="http://purl.uniprot.org/citations/17912370"/>
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<citation rdf:resource="http://purl.uniprot.org/citations/18987218"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.318#SIPC5E4375905480424">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>a carboxylate + eugenol + NADP(+) = a coniferyl ester + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.318#SIPAD9288C2825B6DBB">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>acetate + eugenol + NADP(+) = (E)-coniferyl acetate + NADPH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/citations/18208524">
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<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/18208524"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/18208524"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/citations/18987218">
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<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/18987218"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/18987218"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.319">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>isoeugenol synthase</skos:prefLabel>
<skos:altLabel>T-anol/isoeugenol synthase 1</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.319#SIP11A3F79287D96E3B"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.319#SIP5356955A6098ED33"/>
<rdfs:comment>The enzyme acts in the opposite direction.</rdfs:comment>
<rdfs:comment>In Ocimum basilicum (sweet basil), Clarkia breweri, and Petunia hybrida only isoeugenol is formed.</rdfs:comment>
<rdfs:comment>However in Pimpinella anisum (anise) only anol is formed in vivo, although the cloned enzyme does produce isoeugenol.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/16782809"/>
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<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.319#SIP11A3F79287D96E3B">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>acetate + NADP(+) + trans-isoeugenol = (E)-coniferyl acetate + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.319#SIP5356955A6098ED33">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>acetate + NADP(+) + trans-anol = NADPH + trans-coumaryl acetate.</rdfs:label>
</rdf:Description>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/18987218">
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<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/18987218"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.320">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<replaces rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.n7"/>
<skos:prefLabel>benzil reductase [(S)-benzoin forming]</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.320#SIP2AC106CBAADC9380"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.320#SIPECF9524C24E78F73"/>
<rdfs:comment>The enzyme also reduces 1-phenylpropane-1,2-dione.</rdfs:comment>
<rdfs:comment>The enzyme from Bacillus cereus in addition reduces 1,4-naphthoquinone and 1-(4-methylphenyl)-2-phenylethane-1,2-dione with high efficiency.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/11745140"/>
<citation rdf:resource="http://purl.uniprot.org/citations/11796169"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.320#SIP2AC106CBAADC9380">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(S)-benzoin + NADP(+) = benzil + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.320#SIPECF9524C24E78F73">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>2-hydroxy-1-phenyl-1-propanone + NADP(+) = 1-phenyl-1,2-propanedione + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/11745140">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/11745140"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/citations/11796169">
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<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/11796169"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.321">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>benzil reductase [(R)-benzoin forming]</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.321#SIPD41F31DBCE6A4C23"/>
<rdfs:comment>The enzyme from the bacterium Xanthomonas oryzae is able to reduce enantioselectively only one of the two carbonyl groups of benzil to give optically active (R)-benzoin.</rdfs:comment>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.321#SIPD41F31DBCE6A4C23">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(R)-benzoin + NADP(+) = benzil + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.322">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>(-)-endo-fenchol dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.322#SIP08034A828A0797E8"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.322#SIP3D028CEB4B1A5289"/>
<rdfs:comment>Isolated from the plant Foeniculum vulgare (fennel).</rdfs:comment>
<rdfs:comment>NADH is slightly preferred to NADPH.</rdfs:comment>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.322#SIP08034A828A0797E8">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(1S,2S,4R)-endo-fenchol + NAD(+) = (1S,4R)-fenchone + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.322#SIP3D028CEB4B1A5289">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(1S,2S,4R)-endo-fenchol + NADP(+) = (1S,4R)-fenchone + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.323">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>(+)-thujan-3-ol dehydrogenase</skos:prefLabel>
<skos:altLabel>D-3-thujanol dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.323#SIP4FB09BA620B9EDED"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.323#SIP565E8E406BF63249"/>
<rdfs:comment>Isolated from the plant Tanacetum vulgare (tansy).</rdfs:comment>
<rdfs:comment>NADH is preferred to NADPH.</rdfs:comment>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.323#SIP4FB09BA620B9EDED">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(+)-thujan-3-ol + NADP(+) = (+)-thujan-3-one + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.323#SIP565E8E406BF63249">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(+)-thujan-3-ol + NAD(+) = (+)-thujan-3-one + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.324">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>8-hydroxygeraniol dehydrogenase</skos:prefLabel>
<skos:altLabel>8-hydroxygeraniol oxidoreductase</skos:altLabel>
<skos:altLabel>CYP76B10</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.324#SIP9628ADFBCCF4AC9B"/>
<rdfs:comment>The enzyme catalyzes the oxidation of (6E)-8-hydroxygeraniol to (6E)-8-oxogeranial via either (6E)-8-hydroxygeranial or (6E)-8-oxogeraniol.</rdfs:comment>
<rdfs:comment>Also acts on geraniol, nerol and citronellol.</rdfs:comment>
<rdfs:comment>May be identical to EC 1.1.1.183.</rdfs:comment>
<rdfs:comment>The recommended numbering of geraniol gives 8-hydroxygeraniol as the substrate rather than 10-hydroxygeraniol.</rdfs:comment>
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<rdfs:label>(6E)-8-hydroxygeraniol + 2 NADP(+) = (6E)-8-oxogeranial + 2 H(+) + 2 NADPH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.325">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>sepiapterin reductase (L-threo-7,8-dihydrobiopterin forming)</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.325#SIPA81FBB56934AFFC2"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.325#SIP4E40B6A6F8B08880"/>
<rdfs:comment>This enzyme, isolated from the bacterium Chlorobium tepidum, catalyzes the final step in the de novo synthesis of tetrahydrobiopterin from GTP.</rdfs:comment>
<rdfs:comment>Cf. EC 1.1.1.153.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/10333495"/>
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<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.325#SIPA81FBB56934AFFC2">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>L-threo-7,8-dihydrobiopterin + NADP(+) = H(+) + NADPH + sepiapterin.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.325#SIP4E40B6A6F8B08880">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>L-threo-tetrahydrobiopterin + 2 NADP(+) = 6-pyruvoyl-5,6,7,8-tetrahydropterin + 2 H(+) + 2 NADPH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.326">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>zerumbone synthase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.326#SIP0F6A81613B229241"/>
<rdfs:comment>The enzyme was cloned from shampoo ginger, Zingiber zerumbet.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/21668645"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.326#SIP0F6A81613B229241">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>10-hydroxy-alpha-humulene + NAD(+) = H(+) + NADH + zerumbone.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.327">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>5-exo-hydroxycamphor dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.327#SIPF7FE9000D73DA36D"/>
<rdfs:comment>Isolated from Pseudomonas putida, and involved in degradation of (+)-camphor.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/2613690"/>
<citation rdf:resource="http://purl.uniprot.org/citations/4351810"/>
<citation rdf:resource="http://purl.uniprot.org/citations/8334169"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.327#SIPF7FE9000D73DA36D">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(1R,4R,5R)-5-hydroxycamphor + NAD(+) = (1R,4R)-bornane-2,5-dione + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.328">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>nicotine blue oxidoreductase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.328#SIPB2043D79372561EB"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.328#SIP1EEEBBCCCE72FF58"/>
<rdfs:comment>The enzyme, characterized from the nicotine degrading bacterium Arthrobacter nicotinovorans, catalyzes the reduction of 'nicotine blue' to its hydroquinone form (the opposite direction from that shown).</rdfs:comment>
<rdfs:comment>Nicotine blue is the name given to the compound formed by the autocatalytic condensation of two molecules of 2,3,6-trihydroxypyridine, an intermediate in the nicotine degradation pathway.</rdfs:comment>
<rdfs:comment>The main role of the enzyme may be to prevent the intracellular formation of nicotine blue semiquinone radicals, which by redox cycling would lead to the formation of toxic reactive oxygen species.</rdfs:comment>
<rdfs:comment>The enzyme possesses a slight preference for NADH over NADPH.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/17293530"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.328#SIPB2043D79372561EB">
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<rdfs:label>3,3'-bipyridine-2,2',5,5',6,6'-hexol + NADP(+) = (E)-2,2',5,5'-tetrahydroxy-6H,6'H-(3,3'-bipyridinylidene)-6,6'-dione + 3 H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.328#SIP1EEEBBCCCE72FF58">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>3,3'-bipyridine-2,2',5,5',6,6'-hexol + NAD(+) = (E)-2,2',5,5'-tetrahydroxy-6H,6'H-(3,3'-bipyridinylidene)-6,6'-dione + 3 H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.329">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>2-deoxy-scyllo-inosamine dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.329#SIPE0866E53C1ACA1AA"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.329#SIP7F68EDBD44EA2414"/>
<rdfs:comment>Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, neomycin and ribostamycin.</rdfs:comment>
<rdfs:comment>Cf. EC 1.1.99.38.</rdfs:comment>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.329#SIPE0866E53C1ACA1AA">
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<rdfs:label>2-deoxy-scyllo-inosamine + NADP(+) = 3-amino-2,3-dideoxy-scyllo-inosose + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.329#SIP7F68EDBD44EA2414">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>2-deoxy-scyllo-inosamine + NAD(+) = 3-amino-2,3-dideoxy-scyllo-inosose + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.330">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<replaces rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.n13"/>
<replaces rdf:resource="http://purl.uniprot.org/enzyme/2.3.1.119"/>
<skos:prefLabel>very-long-chain 3-oxoacyl-CoA reductase</skos:prefLabel>
<skos:altLabel>very-long-chain 3-ketoacyl-CoA reductase</skos:altLabel>
<skos:altLabel>very-long-chain beta-ketoacyl-CoA reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.330#SIPB682820518832AF0"/>
<rdfs:comment>The second component of the elongase, a microsomal protein complex responsible for extending palmitoyl-CoA and stearoyl-CoA (and modified forms thereof) to very-long-chain acyl CoAs.</rdfs:comment>
<rdfs:comment>The enzyme is active with substrates with chain length of C16 to C34, depending on the species.</rdfs:comment>
<rdfs:comment>Cf. EC 2.3.1.199, EC 4.2.1.134 and EC 1.3.1.93.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/11792704"/>
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<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.330#SIPB682820518832AF0">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>a very-long-chain (3R)-3-hydroxyacyl-CoA + NADP(+) = a very-long-chain 3-oxoacyl-CoA + H(+) + NADPH.</rdfs:label>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.331">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>secoisolariciresinol dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.331#SIPAFFD43773728B74A"/>
<rdfs:comment>Isolated from the plants Forsythia intermedia and Podophyllum peltatum.</rdfs:comment>
<rdfs:comment>An intermediate lactol is detected in vitro.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/11278426"/>
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<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.331#SIPAFFD43773728B74A">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(-)-secoisolariciresinol + 2 NAD(+) = (-)-matairesinol + 2 H(+) + 2 NADH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.332">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>chanoclavine-I dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.332#SIPEAE133E2186CAE59"/>
<rdfs:comment>The enzyme catalyzes a step in the pathway of ergot alkaloid biosynthesis in certain fungi.</rdfs:comment>
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<citation rdf:resource="http://purl.uniprot.org/citations/22403186"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdfs:label>chanoclavine-I + NAD(+) = chanoclavine-I aldehyde + H(+) + NADH.</rdfs:label>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.333">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase</skos:prefLabel>
<skos:altLabel>decaprenylphospho-beta-D-ribofuranose 2'-epimerase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.333#SIPD4C5305A3E2E0E68"/>
<rdfs:comment>The reaction is catalyzed in the reverse direction.</rdfs:comment>
<rdfs:comment>The enzyme, isolated from the bacterium Mycobacterium smegmatis, is involved, along with EC 1.1.98.3, in the epimerization of trans,octacis-decaprenylphospho-beta-D-ribofuranose to trans,octacis-decaprenylphospho-beta-D-arabinoofuranose, the arabinosyl donor for the biosynthesis of mycobacterial cell wall arabinan polymers.</rdfs:comment>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.333#SIPD4C5305A3E2E0E68">
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<rdfs:label>NAD(+) + trans,octa-cis-decaprenylphospho-beta-D-arabinofuranose = H(+) + NADH + trans,octa-cis-decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.334">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>methylecgonone reductase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.334#SIPFB58ADBDC9050D91"/>
<rdfs:comment>The enzyme from the plant Erythroxylum coca catalyzes the penultimate step in the biosynthesis of cocaine.</rdfs:comment>
<rdfs:comment>In vivo the reaction proceeds in the opposite direction.</rdfs:comment>
<rdfs:comment>With NADH instead of NADPH the reaction rate is reduced to 14%.</rdfs:comment>
<rdfs:comment>The enzyme also reduces tropinone, nortropinone and 6-hydroxytropinone but with lower reaction rates.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/22665766"/>
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<rdfs:label>ecgonine methyl ester + NADP(+) = ecgonone methyl ester + H(+) + NADPH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.335">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.335#SIPC7AAC14CB9251885"/>
<rdfs:comment>This enzyme participates in the biosynthetic pathway for UDP-alpha-D-ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-mannuronic acid), an important precursor of B-band lipopolysaccharide.</rdfs:comment>
<rdfs:comment>The enzymes from Pseudomonas aeruginosa serotype O5 and Thermus thermophilus form a complex with the the enzyme catalyzing the next step the pathway (EC 2.6.1.98).</rdfs:comment>
<rdfs:comment>The enzyme also possesses an EC 1.1.99.2 activity, and utilizes the 2-oxoglutarate produced by EC 2.6.1.98 to regenerate the tightly bound NAD(+).</rdfs:comment>
<rdfs:comment>The enzymes from Bordetella pertussis and Chromobacterium violaceum do not bind NAD(+) as tightly and do not require 2-oxoglutarate to function.</rdfs:comment>
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<rdfs:label>NAD(+) + UDP-N-2-acetamido-2-deoxy-alpha-D-glucuronate = H(+) + NADH + UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.336">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<replaces rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.n3"/>
<skos:prefLabel>UDP-N-acetyl-D-mannosamine dehydrogenase</skos:prefLabel>
<skos:altLabel>UDP-ManNAc 6-dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.336#SIP0317E4DC0338A735"/>
<rdfs:comment>Part of the pathway for acetamido sugar biosynthesis in bacteria and archaea.</rdfs:comment>
<rdfs:comment>The enzyme has no activity with NADP(+).</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/18263721"/>
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<rdfs:label>H2O + 2 NAD(+) + UDP-N-acetyl-alpha-D-mannosamine = 3 H(+) + 2 NADH + UDP-N-acetyl-alpha-D-mannosaminouronate.</rdfs:label>
</rdf:Description>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>L-2-hydroxycarboxylate dehydrogenase (NAD(+))</skos:prefLabel>
<skos:altLabel>(R)-sulfolactate dehydrogenase</skos:altLabel>
<skos:altLabel>L-2-hydroxyacid dehydrogenase (NAD(+))</skos:altLabel>
<skos:altLabel>L-sulfolactate dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.337#SIP6598759D764293F2"/>
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<rdfs:comment>The enzyme from the archaeon Methanocaldococcus jannaschii acts on multiple L-2-hydroxycarboxylates including (2R)-3-sulfolactate, (S)-malate, (S)-lactate, and (S)-2-hydroxyglutarate.</rdfs:comment>
<rdfs:comment>Note that (2R)-3-sulfolactate has the same stereo configuration as (2S)-2-hydroxycarboxylates.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/10850983"/>
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<rdfs:label>a (2S)-2-hydroxycarboxylate + NAD(+) = a 2-oxocarboxylate + H(+) + NADH.</rdfs:label>
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<rdfs:label>(2R)-3-sulfolactate + NAD(+) = 3-sulfopyruvate + H(+) + NADH.</rdfs:label>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.338">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>(2R)-3-sulfolactate dehydrogenase (NADP(+))</skos:prefLabel>
<skos:altLabel>(R)-sulfolactate dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.338#SIP0F782D44A3D1B8F9"/>
<rdfs:comment>The enzyme from the bacterium Chromohalobacter salexigens can only utilize NADP(+).</rdfs:comment>
<rdfs:comment>It functions both biosynthetically in coenzyme M biosynthesis and degradatively, in the degradation of sulfolactate.</rdfs:comment>
<rdfs:comment>It can not use (S)-malate and (S)-lactate.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/20007648"/>
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<rdfs:label>(2R)-3-sulfolactate + NADP(+) = 3-sulfopyruvate + H(+) + NADPH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.339">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>dTDP-6-deoxy-L-talose 4-dehydrogenase (NAD(+))</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.339#SIP11F05BD7747C8193"/>
<rdfs:comment>The enzyme has been characterized from the bacterium Aggregatibacter actinomycetemcomitans, in which it participates in the biosynthesis of the serotype c-specific polysaccharide antigen.</rdfs:comment>
<rdfs:comment>Shows no activity with NADP(+).</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/10702238"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.339#SIP11F05BD7747C8193">
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<rdfs:label>dTDP-6-deoxy-beta-L-talose + NAD(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.340">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>1-deoxy-11beta-hydroxypentalenate dehydrogenase</skos:prefLabel>
<skos:altLabel>1-deoxy-11beta-hydroxypentalenic acid dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.340#SIPF408D75F12231C54"/>
<rdfs:comment>Isolated from the bacterium Streptomyces avermitilis and present in many other Streptomyces species.</rdfs:comment>
<rdfs:comment>Part of the pathway for pentalenolactone biosynthesis.</rdfs:comment>
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<rdfs:label>1-deoxy-11beta-hydroxypentalenate + NAD(+) = 1-deoxy-11-oxopentalenate + H(+) + NADH.</rdfs:label>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.341">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>CDP-abequose synthase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.341#SIP5C26864F5CAD72AF"/>
<rdfs:comment>Isolated from Yersinia pseudotuberculosis and Salmonella enterica.</rdfs:comment>
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<rdfs:label>CDP-alpha-D-abequose + NADP(+) = CDP-4-dehydro-3,6-dideoxy-alpha-D-glucose + H(+) + NADPH.</rdfs:label>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.342">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>CDP-paratose synthase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.342#SIPD83C94ABE17B2E33"/>
<rdfs:comment>The enzyme is involved in synthesis of paratose and tyvelose, unusual 3,6-dideoxyhexose sugars that form part of the O-antigen in the lipopolysaccharides of several enteric bacteria.</rdfs:comment>
<rdfs:comment>Isolated from Salmonella enterica subsp. enterica serovar Typhi (Salmonella typhi).</rdfs:comment>
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<rdfs:label>CDP-alpha-D-paratose + NADP(+) = CDP-4-dehydro-3,6-dideoxy-alpha-D-glucose + H(+) + NADPH.</rdfs:label>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.343">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>phosphogluconate dehydrogenase (NAD(+)-dependent, decarboxylating)</skos:prefLabel>
<skos:altLabel>6-PGDH</skos:altLabel>
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<rdfs:comment>Highly specific for NAD(+).</rdfs:comment>
<rdfs:comment>The enzyme catalyzes both the oxidation and decarboxylation of 6-phospho-D-gluconate.</rdfs:comment>
<rdfs:comment>In the bacterium Methylobacillus flagellatus the enzyme participates in a formaldehyde oxidation pathway.</rdfs:comment>
<rdfs:comment>Cf. EC 1.1.1.44.</rdfs:comment>
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<rdfs:label>6-phospho-D-gluconate + NAD(+) = CO2 + D-ribulose 5-phosphate + NADH.</rdfs:label>
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<skos:prefLabel>dTDP-6-deoxy-L-talose 4-dehydrogenase [NAD(P)(+)]</skos:prefLabel>
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<rdfs:comment>The enzyme works equally well with NAD(+) and NADP(+).</rdfs:comment>
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<rdfs:label>dTDP-6-deoxy-beta-L-talose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH.</rdfs:label>
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<rdfs:label>dTDP-6-deoxy-beta-L-talose + NAD(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADH.</rdfs:label>
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<skos:prefLabel>D-2-hydroxyacid dehydrogenase (NAD(+))</skos:prefLabel>
<skos:altLabel>(R)-2-hydroxyisocaproate dehydrogenase</skos:altLabel>
<skos:altLabel>D-2-hydroxyisocaproate dehydrogenase</skos:altLabel>
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<rdfs:comment>The enzymes, characterized from bacteria (Peptoclostridium difficile, Enterococcus faecalis and from lactic acid bacteria) prefer substrates with a main chain of 5 carbons (such as 4-methyl-2-oxopentanoate) to those with a shorter chain.</rdfs:comment>
<rdfs:comment>It also utilizes phenylpyruvate.</rdfs:comment>
<rdfs:comment>The enzyme from the halophilic archaeon Haloferax mediterranei prefers substrates with a main chain of 3-4 carbons (pyruvate and 2-oxobutanoate).</rdfs:comment>
<rdfs:comment>Cf. EC 1.1.1.272.</rdfs:comment>
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<rdfs:label>a (2R)-2-hydroxycarboxylate + NAD(+) = a 2-oxocarboxylate + H(+) + NADH.</rdfs:label>
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<rdfs:label>(R)-2-hydroxy-4-methylpentanoate + NAD(+) = 4-methyl-2-oxopentanoate + H(+) + NADH.</rdfs:label>
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<skos:prefLabel>2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming)</skos:prefLabel>
<skos:altLabel>2,5-diketo-D-gluconate-reductase</skos:altLabel>
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<rdfs:comment>The enzyme is involved in ketogluconate metabolism, and catalyzes the reaction in vivo in the reverse direction to that shown.</rdfs:comment>
<rdfs:comment>It is used in the commercial microbial production of ascorbate.</rdfs:comment>
<rdfs:comment>cf. EC 1.1.1.274.</rdfs:comment>
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<rdfs:label>2-dehydro-L-idonate + NADP(+) = 2,5-didehydro-D-gluconate + H(+) + NADPH.</rdfs:label>
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<skos:prefLabel>geraniol dehydrogenase (NAD(+))</skos:prefLabel>
<skos:altLabel>GeDH</skos:altLabel>
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<rdfs:comment>The enzyme from the bacterium Castellaniella defragrans is most active in vitro with perillyl alcohol.</rdfs:comment>
<rdfs:comment>The enzyme from the prune mite Carpoglyphus lactis also acts (more slowly) on farnesol but not on nerol.</rdfs:comment>
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<rdfs:label>(2E)-geraniol + NAD(+) = (2E)-geranial + H(+) + NADH.</rdfs:label>
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<skos:prefLabel>(3R)-2'-hydroxyisoflavanone reductase</skos:prefLabel>
<skos:altLabel>vestitone reductase</skos:altLabel>
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<rdfs:comment>This plant enzyme participates in the biosynthesis of the pterocarpan phytoalexins medicarpin, maackiain, and several forms of glyceollin.</rdfs:comment>
<rdfs:comment>The enzyme has a strict stereo specificity for the 3R-isoflavanones.</rdfs:comment>
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<rdfs:label>a (3R,4R)-4,2'-dihydroxyisoflavan + NADP(+) = a (3R)-2'-hydroxyisoflavanone + H(+) + NADPH.</rdfs:label>
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<rdfs:label>(3R,4R)-7,2'-dihydroxy-4'-methoxyisoflavanol + NADP(+) = (3R)-vestitone + H(+) + NADPH.</rdfs:label>
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<skos:prefLabel>norsolorinic acid ketoreductase</skos:prefLabel>
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<rdfs:comment>Involved in the synthesis of aflatoxins in the fungus Aspergillus parasiticus.</rdfs:comment>
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<rdfs:label>(1'S)-averantin + NADP(+) = H(+) + NADPH + norsolorinic acid.</rdfs:label>
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<skos:prefLabel>ureidoglycolate dehydrogenase (NAD(+))</skos:prefLabel>
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<rdfs:comment>Involved in catabolism of purines.</rdfs:comment>
<rdfs:comment>The enzyme from the bacterium Escherichia coli is specific for NAD(+).</rdfs:comment>
<rdfs:comment>Cf. EC 1.1.1.154.</rdfs:comment>
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<rdfs:label>(S)-ureidoglycolate + NAD(+) = H(+) + N-carbamoyl-2-oxoglycine + NADH.</rdfs:label>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>phosphogluconate dehydrogenase [NAD(P)(+)-dependent, decarboxylating]</skos:prefLabel>
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<rdfs:comment>The enzyme participates in the oxidative branch of the pentose phosphate pathway, whose main purpose is to produce reducing power and pentose for biosynthetic reactions.</rdfs:comment>
<rdfs:comment>Unlike EC 1.1.1.44, it is not specific for NADP(+) and can accept both cofactors with similar efficiency.</rdfs:comment>
<rdfs:comment>Cf. EC 1.1.1.343.</rdfs:comment>
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<rdfs:label>6-phospho-D-gluconate + NAD(+) = CO2 + D-ribulose 5-phosphate + NADH.</rdfs:label>
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<rdfs:label>6-phospho-D-gluconate + NADP(+) = CO2 + D-ribulose 5-phosphate + NADPH.</rdfs:label>
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<skos:prefLabel>5'-hydroxyaverantin dehydrogenase</skos:prefLabel>
<skos:altLabel>HAVN dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.352#SIP21D501B1A67CBCBB"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.352#SIPC09FF637E1656178"/>
<rdfs:comment>Isolated from the aflatoxin-producing mold Aspergillus parasiticus.</rdfs:comment>
<rdfs:comment>Involved in aflatoxin biosynthesis.</rdfs:comment>
<rdfs:comment>5'-oxoaverantin will spontaneously form averufin by intramolecular ketalisation.</rdfs:comment>
<rdfs:comment>Cf. EC 4.2.1.142.</rdfs:comment>
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<rdfs:label>(1'S,5'S)-5'-hydroxyaverantin + NAD(+) = (S)-5'-oxoaverantin + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdfs:label>(1'S,5'R)-5'-hydroxyaverantin + NAD(+) = (S)-5'-oxoaverantin + 2 H(+) + NADH.</rdfs:label>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>versiconal hemiacetal acetate reductase</skos:prefLabel>
<skos:altLabel>VHA reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.353#SIP4499168E0AC18560"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.353#SIP45C91BFEA01EEB20"/>
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<rdfs:comment>Isolated from the mold Aspergillus parasiticus.</rdfs:comment>
<rdfs:comment>Involved in a metabolic grid that leads to aflatoxin biosynthesis.</rdfs:comment>
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<rdfs:label>(2S)-versicolorone + NADP(+) = 1'-hydroxyversicolorone + H(+) + NADPH.</rdfs:label>
</rdf:Description>
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<rdfs:label>(3S)-versiconol acetate + NADP(+) = (2S,3S)-versiconal hemiacetal acetate + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.353#SIP93A66ACD3A97D85D">
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<rdfs:label>(S)-versiconol + NADP(+) = (2S-3S)-versiconal hemiacetal + H(+) + NADPH.</rdfs:label>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>farnesol dehydrogenase (NAD(+))</skos:prefLabel>
<skos:altLabel>NAD(+)-farnesol dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.354#SIP8E2B3003C402CB27"/>
<rdfs:comment>The enzyme from the prune mite Carpoglyphus lactis also acts on geraniol with greater activity (cf. 1.1.1.347).</rdfs:comment>
<rdfs:comment>Unlike EC 1.1.1.216, this enzyme cannot use NADP(+) as cofactor.</rdfs:comment>
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<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdfs:label>(2E,6E)-farnesol + NAD(+) = (2E,6E)-farnesal + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>2'-dehydrokanamycin reductase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.355#SIP6BD9525CE3D1DDAE"/>
<rdfs:comment>Found in the bacterium Streptomyces kanamyceticus where it is involved in the conversion of kanamycin B to kanamycin A.</rdfs:comment>
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<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdfs:label>2'-dehydrokanamycin A + H(+) + NADPH = kanamycin A + NADP(+).</rdfs:label>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>GDP-L-colitose synthase</skos:prefLabel>
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<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.356#SIP9EA5B0250CF6B6BB"/>
<rdfs:comment>The enzyme is involved in biosynthesis of L-colitose, a 3,6-dideoxyhexose found in the O-antigen of Gram-negative lipopolysaccharides, where it catalyzes the reaction in the reverse direction.</rdfs:comment>
<rdfs:comment>The enzyme also performs the NAD(P)H-dependent epimerisation at C-5 of the sugar.</rdfs:comment>
<rdfs:comment>The enzyme from Yersinia pseudotuberculosis is Si-specific with respect to NAD(P)H.</rdfs:comment>
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<rdfs:label>GDP-beta-L-colitose + NADP(+) = GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose + H(+) + NADPH.</rdfs:label>
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<rdfs:label>GDP-beta-L-colitose + NAD(+) = GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose + H(+) + NADH.</rdfs:label>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>3alpha-hydroxysteroid 3-dehydrogenase</skos:prefLabel>
<skos:altLabel>3alpha-hydroxysteroid dehydrogenase</skos:altLabel>
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<rdfs:comment>The enzyme acts on multiple 3alpha-hydroxysteroids, such as androsterone and 5 alpha-dihydrotestosterone.</rdfs:comment>
<rdfs:comment>The mammalian enzymes are involved in inactivation of steroid hormones, while the bacterial enzymes are involved in steroid degradation.</rdfs:comment>
<rdfs:comment>This entry stands for enzymes whose stereo-specificity with respect to NAD(+) or NADP(+) is not known (cf. EC 1.1.1.50 and EC 1.1.1.213).</rdfs:comment>
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<rdfs:label>a 3alpha-hydroxysteroid + NADP(+) = a 3-oxosteroid + H(+) + NADPH.</rdfs:label>
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<rdfs:label>a 3alpha-hydroxysteroid + NAD(+) = a 3-oxosteroid + H(+) + NADH.</rdfs:label>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>2-dehydropantolactone reductase</skos:prefLabel>
<skos:altLabel>2-dehydropantoyl-lactone reductase</skos:altLabel>
<skos:altLabel>2-ketopantoyl lactone reductase</skos:altLabel>
<skos:altLabel>2-oxopantoyl lactone reductase</skos:altLabel>
<skos:altLabel>ketopantoyl lactone reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.358#SIPD08E6B969BC8D986"/>
<rdfs:comment>The enzyme participates in an alternative pathway for biosynthesis of (R)-pantothenate (vitamin B5).</rdfs:comment>
<rdfs:comment>This entry covers enzymes whose stereo specificity for NADP(+) is not known (cf. EC 1.1.1.168 and EC 1.1.1.214).</rdfs:comment>
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<rdfs:label>(R)-pantolactone + NADP(+) = 2-dehydropantolactone + H(+) + NADPH.</rdfs:label>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>aldose 1-dehydrogenase [NAD(P)(+)]</skos:prefLabel>
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<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.359#SIP0B0832D01DAC8F7C"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.359#SIPA8FD677859758569"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.359#SIP573AF37EBE72B77E"/>
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<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.359#SIPA31548E25A5E3AF0"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.359#SIP0B4932267B364C4E"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.359#SIPAA81FD84D1AB7017"/>
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<rdfs:comment>The enzyme from the archaeon Sulfolobus solfataricus shows broad specificity toward aldoses (D-glucose, D-galactose, D-xylose, L-arabinose, 6-deoxy-D-glucose, D-fucose) and can utilize NAD(+) and NADP(+) with similar catalytic efficiency.</rdfs:comment>
<rdfs:comment>It is involved in aldose catabolism via the branched variant of the Entner-Doudoroff pathway.</rdfs:comment>
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<rdfs:label>an aldopyranose + NADP(+) = aldono-1,5-lactone + H(+) + NADPH.</rdfs:label>
</rdf:Description>
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<rdfs:label>an aldopyranose + NAD(+) = aldono-1,5-lactone + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.359#SIPA8FD677859758569">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-glucose + NADP(+) = D-glucono-1,5-lactone + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.359#SIP573AF37EBE72B77E">
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<rdfs:label>D-glucose + NAD(+) = D-glucono-1,5-lactone + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.359#SIP0F4396A50B830C07">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-galactose + NADP(+) = D-galactono-1,5-lactone + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.359#SIPA31548E25A5E3AF0">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-galactose + NAD(+) = D-galactono-1,5-lactone + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.359#SIP0B4932267B364C4E">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-xylose + NAD(+) = D-xylono-1,5-lactone + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.359#SIPAA81FD84D1AB7017">
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<rdfs:label>D-xylose + NADP(+) = D-xylono-1,5-lactone + H(+) + NADPH.</rdfs:label>
</rdf:Description>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>alpha-L-arabinopyanose + NAD(+) = H(+) + L-arabinono-1,4-lactone + NADH.</rdfs:label>
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<skos:prefLabel>glucose/galactose 1-dehydrogenase</skos:prefLabel>
<skos:altLabel>dual-specific glucose/galactose dehydrogenase</skos:altLabel>
<skos:altLabel>glucose/galactose dehydrogenase</skos:altLabel>
<skos:altLabel>glucose (galactose) dehydrogenase</skos:altLabel>
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<rdfs:comment>The enzyme from the archaeon Picrophilus torridus is involved in glucose and galactose catabolism via the nonphosphorylative variant of the Entner-Doudoroff pathway.</rdfs:comment>
<rdfs:comment>It shows 20-fold higher activity with NADP(+) compared to NAD(+).</rdfs:comment>
<rdfs:comment>The oxidation of D-glucose and D-galactose is catalyzed at a comparable rate (cf. EC 1.1.1.119 and EC 1.1.1.120).</rdfs:comment>
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<rdfs:label>D-glucose + NADP(+) = D-glucono-1,5-lactone + H(+) + NADPH.</rdfs:label>
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<rdfs:label>D-galactose + NADP(+) = D-galactono-1,5-lactone + H(+) + NADPH.</rdfs:label>
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<skos:prefLabel>glucose-6-phosphate 3-dehydrogenase</skos:prefLabel>
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<rdfs:comment>The enzyme, found in the bacterium Bacillus subtilis, is involved in a kanosamine biosynthesis pathway.</rdfs:comment>
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<rdfs:label>D-glucose 6-phosphate + NAD(+) = 3-dehydro-D-glucose 6-phosphate + H(+) + NADH.</rdfs:label>
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<skos:prefLabel>aklaviketone reductase</skos:prefLabel>
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<rdfs:comment>The enzyme is involved in the synthesis of the aklavinone aglycone, a common precursor for several anthracycline antibiotics including aclacinomycins, daunorubicin and doxorubicin.</rdfs:comment>
<rdfs:comment>The enzyme from the Gram-negative bacterium Streptomyces sp. C5 produces daunomycin.</rdfs:comment>
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<rdfs:label>aklavinone + NADP(+) = aklaviketone + 2 H(+) + NADPH.</rdfs:label>
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<skos:prefLabel>glucose-6-phosphate dehydrogenase [NAD(P)(+)]</skos:prefLabel>
<skos:altLabel>G6PD</skos:altLabel>
<skos:altLabel>G6PDH</skos:altLabel>
<skos:altLabel>Glc6PD</skos:altLabel>
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<rdfs:comment>The enzyme catalyzes a step of the pentose phosphate pathway.</rdfs:comment>
<rdfs:comment>The enzyme from the Gram-positive bacterium Leuconostoc mesenteroides prefers NADP(+) while the enzyme from the Gram-negative bacterium Gluconacetobacter xylinus prefers NAD(+).</rdfs:comment>
<rdfs:comment>Cf. EC 1.1.1.49 and EC 1.1.1.388.</rdfs:comment>
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<rdfs:label>D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH.</rdfs:label>
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<rdfs:label>D-glucose 6-phosphate + NAD(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADH.</rdfs:label>
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<skos:prefLabel>dTDP-4-dehydro-6-deoxy-alpha-D-gulose 4-ketoreductase</skos:prefLabel>
<skos:altLabel>dTDP-4-dehydro-6-deoxygulose reductase</skos:altLabel>
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<rdfs:comment>The enzyme forms an activated deoxy-alpha-D-allose, which is converted to mycinose after attachment to the aglycones of several macrolide antibiotics, including tylosin, chalcomycin, dihydrochalcomycin, and mycinamicin II.</rdfs:comment>
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<rdfs:label>dTDP-6-deoxy-alpha-D-allose + NAD(+) = dTDP-4-dehydro-6-deoxy-alpha-D-allose + H(+) + NADH.</rdfs:label>
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<rdfs:label>dTDP-6-deoxy-alpha-D-allose + NADP(+) = dTDP-4-dehydro-6-deoxy-alpha-D-allose + H(+) + NADPH.</rdfs:label>
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<replaces rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.n9"/>
<skos:prefLabel>D-galacturonate reductase</skos:prefLabel>
<skos:altLabel>GalUR</skos:altLabel>
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<rdfs:comment>The enzyme from plants is involved in ascorbic acid (vitamin C) biosynthesis.</rdfs:comment>
<rdfs:comment>The enzyme from the fungus Trichoderma reesei (Hypocrea jecorina) is involved in a eukaryotic degradation pathway of D-galacturonate.</rdfs:comment>
<rdfs:comment>It is also active with D-glucuronate and glyceraldehyde.</rdfs:comment>
<rdfs:comment>Neither enzyme shows any activity with NADH.</rdfs:comment>
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<rdfs:label>L-galactonate + NADP(+) = aldehydo-D-galacturonate + H(+) + NADPH.</rdfs:label>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<replaces rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.n8"/>
<skos:prefLabel>L-idonate 5-dehydrogenase (NAD(+))</skos:prefLabel>
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<rdfs:comment>Involved in the catabolism of ascorbate (vitamin C) to tartrate.</rdfs:comment>
<rdfs:comment>No activity is observed with NADP(+) (cf. EC 1.1.1.264).</rdfs:comment>
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<rdfs:label>L-idonate + NAD(+) = 5-dehydro-D-gluconate + H(+) + NADH.</rdfs:label>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>UDP-2-acetamido-2,6-beta-L-arabino-hexul-4-ose reductase</skos:prefLabel>
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<rdfs:comment>Part of the biosynthesis of UDP-N-acetyl-L-fucosamine.</rdfs:comment>
<rdfs:comment>Isolated from the bacteria Pseudomonas aeruginosa and Staphylococcus aureus.</rdfs:comment>
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<rdfs:label>H(+) + NADPH + UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose = NADP(+) + UDP-2-acetamido-2,6-dideoxy-beta-L-talose.</rdfs:label>
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<rdfs:label>H(+) + NADH + UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose = NAD(+) + UDP-2-acetamido-2,6-dideoxy-beta-L-talose.</rdfs:label>
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<skos:prefLabel>6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase</skos:prefLabel>
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<rdfs:comment>The enzyme participates in the central benzoyl-CoA degradation pathway of some anaerobic bacteria such as Thauera aromatica.</rdfs:comment>
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<rdfs:label>6-hydroxycyclohex-1-ene-1-carbonyl-CoA + NAD(+) = 6-oxocyclohex-1-ene-1-carbonyl-CoA + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<replaces rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.n6"/>
<skos:prefLabel>D-chiro-inositol 1-dehydrogenase</skos:prefLabel>
<skos:altLabel>DCI 1-dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.369#SIP5469A6C5257A3575"/>
<rdfs:comment>The enzyme, found in the bacterium Bacillus subtilis, also catalyzes the reaction of EC 1.1.1.18 and can also use D-glucose and D-xylose.</rdfs:comment>
<rdfs:comment>It shows trace activity with D-ribose and D-fructose.</rdfs:comment>
<rdfs:comment>It is part of a myo-inositol/D-chiro-inositol degradation pathway leading to acetyl-CoA.</rdfs:comment>
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<rdfs:label>1D-chiro-inositol + NAD(+) = H(+) + NADH + scyllo-inosine.</rdfs:label>
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<skos:prefLabel>scyllo-inositol 2-dehydrogenase (NAD(+))</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.370#SIPF0C971CC996A81AF"/>
<rdfs:comment>The enzyme, found in the bacterium Bacillus subtilis, has no activity with NADP(+) (cf. EC 1.1.1.371).</rdfs:comment>
<rdfs:comment>It is part of a scyllo-inositol degradation pathway leading to acetyl-CoA.</rdfs:comment>
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<rdfs:label>NAD(+) + scyllo-inositol = H(+) + NADH + scyllo-inosose.</rdfs:label>
</rdf:Description>
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<skos:prefLabel>scyllo-inositol 2-dehydrogenase (NADP(+))</skos:prefLabel>
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<rdfs:comment>The enzyme, found in the bacterium Bacillus subtilis, has no activity with NAD(+) (cf. EC 1.1.1.370).</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/20133360"/>
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<rdfs:label>NADP(+) + scyllo-inositol = H(+) + NADPH + scyllo-inosose.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.372">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>D/L-glyceraldehyde reductase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.372#SIPA84B5B8BAC776E19"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.372#SIP33BFD81643982BE9"/>
<rdfs:comment>The enzyme takes part in a D-galacturonate degradation pathway in the fungi Aspergillus niger and Trichoderma reesei (Hypocrea jecorina).</rdfs:comment>
<rdfs:comment>It has equal activity with D- and L-glyceraldehyde, and can also reduce glyoxal and methylglyoxal.</rdfs:comment>
<rdfs:comment>The reaction is only observed in the direction of glyceraldehyde reduction.</rdfs:comment>
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<rdfs:label>glycerol + NADP(+) = H(+) + L-glyceraldehyde + NADPH.</rdfs:label>
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<rdfs:label>glycerol + NADP(+) = D-glyceraldehyde + H(+) + NADPH.</rdfs:label>
</rdf:Description>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>sulfolactaldehyde 3-reductase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.373#SIPCC3F7ACE4F20A6A9"/>
<rdfs:comment>The enzyme, characterized from the bacterium Escherichia coli, is involved in the degradation pathway of sulfoquinovose, the polar headgroup of sulfolipids found in the photosynthetic membranes of all higher plants, mosses, ferns, algae, and most photosynthetic bacteria, as well as the surface layer of some archaea.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/24463506"/>
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<rdfs:label>(2S)-3-sulfopropanediol + NAD(+) = (2S)-3-sulfolactaldehyde + H(+) + NADH.</rdfs:label>
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<dcterms:identifier>doi:10.1038/nature12947</dcterms:identifier>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.374">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>UDP-N-acetylglucosamine 3-dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.374#SIP158743B7B93F9D57"/>
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<rdfs:label>NAD(+) + UDP-N-acetyl-alpha-D-glucosamine = H(+) + NADH + UDP-2-acetamido-3-dehydro-2-deoxy-alpha-D-glucopyranose.</rdfs:label>
</rdf:Description>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>L-2-hydroxycarboxylate dehydrogenase [NAD(P)(+)]</skos:prefLabel>
<skos:altLabel>lactate/malate dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.375#SIP6598759D764293F2"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.375#SIP60F42B84D3DC84C5"/>
<rdfs:comment>The enzyme from the archaeon Methanocaldococcus jannaschii catalyzes the reversible oxidation of (2R)-3-sulfolactate and (S)-malate to 3-sulfopyruvate and oxaloacetate, respectively (note that (2R)-3-sulfolactate has the same stereochemical configuration as (2S)-2-hydroxycarboxylates).</rdfs:comment>
<rdfs:comment>The enzyme can use both NADH and NADPH, although activity is higher with NADPH.</rdfs:comment>
<rdfs:comment>The oxidation of (2R)-3-sulfolactate was observed only in the presence of NADP(+).</rdfs:comment>
<rdfs:comment>The same organism also possesses an NAD(+)-specific enzyme with similar activity, cf. EC 1.1.1.337.</rdfs:comment>
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<rdfs:label>a (2S)-2-hydroxycarboxylate + NAD(+) = a 2-oxocarboxylate + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdfs:label>a (2S)-2-hydroxycarboxylate + NADP(+) = a 2-oxocarboxylate + H(+) + NADPH.</rdfs:label>
</rdf:Description>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>L-arabinose 1-dehydrogenase [NAD(P)(+)]</skos:prefLabel>
<skos:altLabel>L-arabino-aldose dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.376#SIP5394FF321C0605A3"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.376#SIPDA52C8A33536D054"/>
<rdfs:comment>The enzymes from the bacterium Azospirillum brasilense and the archaeon Haloferax volcanii are part of the L-arabinose degradation pathway and prefer NADP(+) over NAD(+).</rdfs:comment>
<rdfs:comment>In vitro the enzyme from Azospirillum brasilense shows also high catalytic efficiency with D-galactose.</rdfs:comment>
<rdfs:comment>The enzyme is specific for alpha-L-arabinopyranose.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/16326697"/>
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<rdfs:label>alpha-L-arabinopyanose + NAD(+) = H(+) + L-arabinono-1,4-lactone + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.376#SIPDA52C8A33536D054">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>alpha-L-arabinopyanose + NADP(+) = H(+) + L-arabinono-1,4-lactone + NADPH.</rdfs:label>
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<dcterms:identifier>doi:10.1007/s00792-013-0572-2</dcterms:identifier>
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<dcterms:identifier>doi:10.1007/s00253-014-6039-2</dcterms:identifier>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.377">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>L-rhamnose 1-dehydrogenase (NADP(+))</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.377#SIP2022816F183C4387"/>
<rdfs:comment>The enzyme from the archaeon Thermoplasma acidophilum is part of the non-phosphorylative degradation pathway for L-rhamnose.</rdfs:comment>
<rdfs:comment>The enzyme differs in cofactor specificity from EC 1.1.1.173, which is specific for NAD(+).</rdfs:comment>
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<rdfs:label>L-rhamnofuranose + NADP(+) = H(+) + L-rhamnono-1,4-lactone + NADPH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.378">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>L-rhamnose 1-dehydrogenase [NAD(P)(+)]</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.378#SIP3A5089B26BC560B2"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.378#SIP2022816F183C4387"/>
<rdfs:comment>The enzyme, which occurs in the bacteria Azotobacter vinelandii and Sphingomonas sp. SKA58, is part of the non-phosphorylative degradation pathway for L-rhamnose.</rdfs:comment>
<rdfs:comment>The enzyme differs in cofactor specificity from EC 1.1.1.173, which is specific for NAD(+) and EC 1.1.1.377.</rdfs:comment>
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<rdfs:label>L-rhamnofuranose + NAD(+) = H(+) + L-rhamnono-1,4-lactone + NADH.</rdfs:label>
</rdf:Description>
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<rdfs:label>L-rhamnofuranose + NADP(+) = H(+) + L-rhamnono-1,4-lactone + NADPH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.379">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>(R)-mandelate dehydrogenase</skos:prefLabel>
<skos:altLabel>D-mandelate dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.379#SIP605043716CD334E8"/>
<rdfs:comment>The enzyme, found in bacteria and fungi, can also accept a number of substituted mandelate derivatives, such as 3-hydroxymandelate, 4-hydroxymandelate, 2-methoxymandelate, 4-hydroxy-3-methoxymandelate and 3-hydroxy-4-methoxymandelate.</rdfs:comment>
<rdfs:comment>The enzyme has no activity with (S)-mandelate (cf. EC 1.1.99.31).</rdfs:comment>
<rdfs:comment>The enzyme transfers the pro-R hydrogen from NADH.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/1731758"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.379#SIP605043716CD334E8">
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<rdfs:label>(R)-mandelate + NAD(+) = H(+) + NADH + phenylglyoxylate.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/1731758">
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<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/1731758"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.380">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>L-gulonate 5-dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.380#SIP93B8FDD543754699"/>
<rdfs:comment>The enzyme, characterized from the bacterium Halomonas elongata, participates in a pathway for L-gulonate degradation.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/6993236"/>
<citation rdf:resource="http://purl.uniprot.org/citations/25145794"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.380#SIP93B8FDD543754699">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>L-gulonate + NAD(+) = H(+) + keto-D-fructuronate + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/6993236">
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<rdf:Description rdf:about="http://purl.uniprot.org/citations/25145794">
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.381">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>3-hydroxy acid dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.381#SIP1978C6CE422387A3"/>
<rdfs:comment>The enzyme, purified from the bacterium Escherichia coli and the yeast Saccharomyces cerevisiae, shows activity with a range of 3- and 4-carbon 3-hydroxy acids.</rdfs:comment>
<rdfs:comment>The highest activity is seen with L-allo-threonine and D-threonine.</rdfs:comment>
<rdfs:comment>The enzyme from E. coli also shows high activity with L-serine, D-serine, (S)-3-hydroxy-2-methylpropanoate and (R)-3-hydroxy-2-methylpropanoate.</rdfs:comment>
<rdfs:comment>The enzyme has no activity with NAD(+) or L-threonine (cf. EC 1.1.1.103).</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/12535615"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.381#SIP1978C6CE422387A3">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>L-allo-threonine + NADP(+) = aminoacetone + CO2 + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/12535615">
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.382">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>ketol-acid reductoisomerase (NAD(+))</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.382#SIP558E5B396783E50B"/>
<rdfs:comment>The enzyme, characterized from the bacteria Thermacetogenium phaeum and Desulfococcus oleovorans and from the archaeon Archaeoglobus fulgidus, is specific for NADH (cf. EC 1.1.1.86 and EC 1.1.1.383).</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/25172159"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.382#SIP558E5B396783E50B">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(2R)-2,3-dihydroxy-3-methylbutanoate + NAD(+) = (2S)-2-acetolactate + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/25172159">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/25172159"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.383">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>ketol-acid reductoisomerase [NAD(P)(+)]</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.383#SIP558E5B396783E50B"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.383#SIPFDB241690BFDBAB5"/>
<rdfs:comment>The enzyme, characterized from the bacteria Hydrogenobaculum sp. and Syntrophomonas wolfei subsp. wolfei and from the archaea Metallosphaera sedula and Ignisphaera aggregans, can use both NADH and NADPH with similar efficiency (cf. EC 1.1.1.86 and EC 1.1.1.382).</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/25172159"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.383#SIP558E5B396783E50B">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(2R)-2,3-dihydroxy-3-methylbutanoate + NAD(+) = (2S)-2-acetolactate + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.383#SIPFDB241690BFDBAB5">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-acetolactate + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/25172159">
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.384">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose 3-reductase</skos:prefLabel>
<skos:altLabel>dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose 3-oxidoreductase</skos:altLabel>
<skos:altLabel>dTDP-4-keto-2,6-dideoxy-D-glucose 3-oxidoreductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.384#SIP08ECA58A8902F5BA"/>
<rdfs:comment>The enzyme is involved in the biosynthesis of several deoxysugars, including L-digitoxose, L- and D-olivose, L-oliose, D-mycarose and forosamine.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/11932454"/>
<citation rdf:resource="http://purl.uniprot.org/citations/18345667"/>
<citation rdf:resource="http://purl.uniprot.org/citations/21598943"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.384#SIP08ECA58A8902F5BA">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + NADP(+) = dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/11932454">
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<rdf:Description rdf:about="http://purl.uniprot.org/citations/18345667">
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/21598943">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/21598943"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/21598943"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.385">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>dihydroanticapsin 7-dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.385#SIPE286C64894860A79"/>
<rdfs:comment>The enzyme, characterized from the bacterium Bacillus subtilis, is involved in the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin, composed of L-alanine and L-anticapsin.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/23317005"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.385#SIPE286C64894860A79">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>L-dihydroanticapsin + NAD(+) = H(+) + L-anticapsin + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/23317005">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/23317005"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/23317005"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.386">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>ipsdienol dehydrogenase</skos:prefLabel>
<skos:altLabel>IDOLDH</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.386#SIPA8035867C8489386"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.386#SIPCE3FCFE1816E39F2"/>
<rdfs:comment>The enzyme is involved in pheromone production by the pine engraver beetle, Ips pini.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/22101251"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.386#SIPA8035867C8489386">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(4R)-ipsdienol + NADP(+) = H(+) + ipsdienone + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.386#SIPCE3FCFE1816E39F2">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(4R)-ipsdienol + NAD(+) = H(+) + ipsdienone + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/22101251">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/22101251"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.387">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>L-serine 3-dehydrogenase (NAD(+))</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.387#SIP710D6F7AFA36BEDE"/>
<rdfs:comment>The enzyme, purified from the bacterium Pseudomonas aeruginosa, also shows activity with L-threonine (cf. EC 1.1.1.103).</rdfs:comment>
<rdfs:comment>The enzyme has only very low activity with NADP(+) (cf. EC 1.1.1.276).</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/22128181"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.387#SIP710D6F7AFA36BEDE">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>L-serine + NAD(+) = aminoacetaldehyde + CO2 + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/22128181">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/22128181"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/22128181"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.388">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>glucose-6-phosphate dehydrogenase (NAD(+))</skos:prefLabel>
<skos:altLabel>Glc6PDH</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.388#SIP9B76BD57084D8A84"/>
<rdfs:comment>The enzyme catalyzes a step of the pentose phosphate pathway.</rdfs:comment>
<rdfs:comment>The enzyme from the archaeon Haloferax volcanii is specific for NAD(+).</rdfs:comment>
<rdfs:comment>Cf. EC 1.1.1.363 and EC 1.1.1.49.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/25836736"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.388#SIP9B76BD57084D8A84">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-glucose 6-phosphate + NAD(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/25836736">
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.389">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>2-dehydro-3-deoxy-L-galactonate 5-dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.389#SIP2B108B47FB4CA955"/>
<rdfs:comment>The enzyme, characterized from agarose-degrading bacteria, is involved in a degradation pathway for 3,6-anhydro-alpha-L-galactopyranose, a major component of the polysaccharides of red macroalgae.</rdfs:comment>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.389#SIP2B108B47FB4CA955">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>2-dehydro-3-deoxy-L-galactonate + NAD(+) = 3-deoxy-D-glycero-2,5-hexodiulosonate + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.390">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>sulfoquinovose 1-dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.390#SIPE8D7CD40FBF83D07"/>
<rdfs:comment>The enzyme, characterized from the bacterium Pseudomonas putida SQ1, participates in a sulfoquinovose degradation pathway.</rdfs:comment>
<rdfs:comment>Activity with NADP(+) is only 4% of that with NAD(+).</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/26195800"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.390#SIPE8D7CD40FBF83D07">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>6-sulfo-D-quinovose + NAD(+) = 6-deoxy-6-sulfo-D-glucono-1,5-lactone + H(+) + NADH.</rdfs:label>
</rdf:Description>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.391">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>3beta-hydroxycholanate 3-dehydrogenase (NAD(+))</skos:prefLabel>
<skos:altLabel>3beta-hydroxysteroid dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.391#SIP46A59556521716A7"/>
<rdfs:comment>This bacterial enzyme is involved, along with EC 1.1.1.52 or EC 1.1.1.392, in the modification of secondary bile acids to form 3beta-bile acids (also known as iso-bile acids).</rdfs:comment>
<rdfs:comment>The enzyme catalyzes the reaction in the reduction direction in vivo.</rdfs:comment>
<rdfs:comment>Also acts on related 3-oxo bile acids.</rdfs:comment>
<rdfs:comment>Cf. 1.1.1.393.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/2752021"/>
<citation rdf:resource="http://purl.uniprot.org/citations/2764572"/>
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<rdfs:label>3-oxo-5beta-cholan-24-oate + H(+) + NADH = isolithocholate + NAD(+).</rdfs:label>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.392">
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<skos:prefLabel>3alpha-hydroxycholanate dehydrogenase (NADP(+))</skos:prefLabel>
<skos:altLabel>alpha-hydroxy-cholanate dehydrogenase</skos:altLabel>
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<rdfs:comment>This bacterial enzyme is involved in the modification of secondary bile acids to form 3beta-bile acids (also known as iso-bile acids) via a 3-oxo intermediate.</rdfs:comment>
<rdfs:comment>The enzyme catalyzes a reversible reaction in vitro.</rdfs:comment>
<rdfs:comment>Also acts on related bile acids.</rdfs:comment>
<rdfs:comment>Cf. EC 1.1.1.52.</rdfs:comment>
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<rdfs:label>lithocholate + NADP(+) = 3-oxo-5beta-cholan-24-oate + H(+) + NADPH.</rdfs:label>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.393">
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<skos:prefLabel>3beta-hydroxycholanate 3-dehydrogenase (NADP(+))</skos:prefLabel>
<skos:altLabel>3beta-hydroxysteroid dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.393#SIPC3486CAE1265ECF5"/>
<rdfs:comment>This bacterial enzyme is involved, along with EC 1.1.1.52 or EC 1.1.1.392, in the modification of secondary bile acids to form 3beta-bile acids (also known as iso-bile acids).</rdfs:comment>
<rdfs:comment>The enzyme catalyzes the reaction in the reduction direction in vivo.</rdfs:comment>
<rdfs:comment>Also acts on related 3-oxo bile acids.</rdfs:comment>
<rdfs:comment>Cf. EC 1.1.1.391.</rdfs:comment>
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<rdfs:label>3-oxo-5beta-cholan-24-oate + H(+) + NADPH = isolithocholate + NADP(+).</rdfs:label>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.394">
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<skos:prefLabel>aurachin B dehydrogenase</skos:prefLabel>
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<rdfs:comment>The enzyme from the bacterium Stigmatella aurantiaca catalyzes the final step in the conversion of aurachin C to aurachin B.</rdfs:comment>
<rdfs:comment>In vivo the enzyme catalyzes the reduction of 4-hydroxy-2-methyl-3-oxo-4-[(2E,6E)-farnesyl]-3,4-dihydroquinoline-1-oxide to form 2-methyl-1-oxo-4-[(2E,6E)-farnesyl]-3,4-dihydroquinoline-3,4-diol (note that the reactions written above proceed from right to left), which then undergoes a spontaneous dehydration to form aurachin B.</rdfs:comment>
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<rdfs:label>aurachin B + H2O + NAD(+) = 4-hydroxy-2-methyl-3-oxo-[(2E,6E)-farnesyl]-3,4-dihydroquinoline 1-oxide + NADH.</rdfs:label>
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<replaces rdf:resource="http://purl.uniprot.org/enzyme/1.17.1.6"/>
<replaces rdf:resource="http://purl.uniprot.org/enzyme/1.17.98.1"/>
<replaces rdf:resource="http://purl.uniprot.org/enzyme/1.17.99.5"/>
<skos:prefLabel>3alpha-hydroxybile acid CoA 3-dehydrogenase</skos:prefLabel>
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<rdfs:comment>This bacterial enzyme is involved in the 7-dehydroxylation process associated with bile acid degradation.</rdfs:comment>
<rdfs:comment>The enzyme has very little activity with unconjugated bile acid substrates.</rdfs:comment>
<rdfs:comment>It has similar activity with choloyl-CoA, chenodeoxycholoyl-CoA, deoxycholoyl-CoA, and lithocholoyl-CoA.</rdfs:comment>
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<rdfs:label>a 3alpha-hydroxy bile acid CoA + NAD(+) = a 3-oxo bile acid CoA + H(+) + NADH.</rdfs:label>
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<rdfs:label>choloyl-CoA + NAD(+) = 7alpha,12alpha-dihydroxy-3-oxochol-24-oyl-CoA + H(+) + NADH.</rdfs:label>
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<rdfs:label>chenodeoxycholoyl-CoA + NAD(+) = 7alpha-hydroxy-3-oxochol-24-oyl-CoA + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdfs:label>deoxycholoyl-CoA + NAD(+) = 12alpha-hydroxy-3-oxocholan-24-oyl-CoA + H(+) + NADH.</rdfs:label>
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<rdfs:label>lithocholoyl-CoA + NAD(+) = 3-oxocholan-24-oyl-CoA + H(+) + NADH.</rdfs:label>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.396">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>bacteriochlorophyllide-a dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.396#SIPABC45721F7DA277F"/>
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<rdfs:comment>The enzyme, together with EC 1.3.7.15 and EC 4.2.1.165, is involved in the conversion of chlorophyllide a to bacteriochlorophyllide a.</rdfs:comment>
<rdfs:comment>The enzymes can act in multiple orders, resulting in the formation of different intermediates, but the final product of the cumulative action of the three enzymes is always bacteriochlorophyllide a.</rdfs:comment>
<rdfs:comment>The enzyme oxidizes a hydroxyl group on ring A, converting it to an oxo group.</rdfs:comment>
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<rdfs:label>3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a + NAD(+) = bacteriochlorophyllide a + H(+) + NADH.</rdfs:label>
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<rdfs:label>3-devinyl-3-(1-hydroxyethyl)chlorophyllide a + NAD(+) = 3-acetyl-3-devinylchlorophyllide a + H(+) + NADH.</rdfs:label>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.397">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>beta-methylindole-3-pyruvate reductase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.397#SIPBE37DE34FF7AA87A"/>
<rdfs:comment>The enzyme, characterized from the bacterium Streptomyces griseus, participates in the biosynthesis of indolmycin, an antibacterial drug that inhibits the bacterial EC 6.1.1.2.</rdfs:comment>
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<rdfs:label>(2S,3R)-2-hydroxy-3-(indol-3-yl)butanoate + NAD(+) = (R)-3-(indol-3-yl)-2-oxobutanoate + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.398">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>2-glutathionyl-2-methylbut-3-en-1-ol dehydrogenase</skos:prefLabel>
<skos:altLabel>4-hydroxy-3-glutathionyl-3-methylbut-1-ene dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.398#SIPB7F2DF7960FAE6A3"/>
<rdfs:comment>The enzyme, characterized from the bacterium Rhodococcus sp. AD45, is involved in isoprene degradation.</rdfs:comment>
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<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdfs:label>2-glutathionyl-2-methylbut-3-en-1-ol + H2O + 2 NAD(+) = 2-glutathionyl-2-methylbut-3-enoate + 3 H(+) + 2 NADH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.399">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>2-oxoglutarate reductase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.399#SIP246E7D403933D44E"/>
<rdfs:comment>The enzyme catalyzes a reversible reaction.</rdfs:comment>
<rdfs:comment>The enzyme from the bacterium Peptoniphilus asaccharolyticus is specific for (R)-2-hydroxyglutarate.</rdfs:comment>
<rdfs:comment>The SerA enzyme from Escherichia coli can also accept (S)-2-hydroxyglutarate with a much higher Km, and also catalyzes the activity of EC 1.1.1.95.</rdfs:comment>
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<rdfs:label>(R)-2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + H(+) + NADH.</rdfs:label>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.400">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>2-methyl-1,2-propanediol dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.400#SIP8F6FCA9281CBCB49"/>
<rdfs:comment>This bacterial enzyme is involved in the degradation pathways of the alkene 2-methylpropene and the fuel oxygenate methyl tert-butyl ether (MTBE), a widely occurring groundwater contaminant.</rdfs:comment>
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<rdfs:label>2-methylpropane-1,2-diol + NAD(+) = 2-hydroxy-2-methylpropanal + H(+) + NADH.</rdfs:label>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.401">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>2-dehydro-3-deoxy-L-rhamnonate dehydrogenase (NAD(+))</skos:prefLabel>
<skos:altLabel>2-keto-3-deoxy-L-rhamnonate dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.401#SIP2710424AE9D73012"/>
<rdfs:comment>The enzyme, characterized from the bacteria Sphingomonas sp. SKA58 and Sulfobacillus thermosulfidooxidans, is involved in the non-phosphorylative degradation pathway for L-rhamnose.</rdfs:comment>
<rdfs:comment>It does not show any detectable activity with NADP(+) or with other aldoses.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/19187228"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.401#SIP2710424AE9D73012">
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<rdfs:label>2-dehydro-3-deoxy-L-rhamnonate + NAD(+) = 2,4-didehydro-3-deoxy-L-rhamnonate + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.402">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>D-erythritol 1-phosphate dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.402#SIP9E3A596AFE568CAC"/>
<rdfs:comment>The enzyme, characterized from the pathogenic bacterium Brucella abortus, which causes brucellosis in livestock, participates in erythritol catabolism.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/163226"/>
<citation rdf:resource="http://purl.uniprot.org/citations/10708387"/>
<citation rdf:resource="http://purl.uniprot.org/citations/25453104"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.402#SIP9E3A596AFE568CAC">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-erythritol 1-phosphate + NADP(+) = D-erythrulose 1-phosphate + H(+) + NADPH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.403">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>D-threitol dehydrogenase (NAD(+))</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.403#SIPC50C0065D507FE0A"/>
<rdfs:comment>The enzyme, characterized from the bacterium Mycobacterium smegmatis, participates in the degradation of D-threitol.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/26560079"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.403#SIPC50C0065D507FE0A">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-threitol + NAD(+) = D-erythrulose + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/26560079">
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.404">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>tetrachlorobenzoquinone reductase</skos:prefLabel>
<skos:altLabel>TCBQ reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.404#SIP7FADEB4269B7EA44"/>
<rdfs:comment>The enzyme, characterized from the bacterium Sphingobium chlorophenolicum, participates in the degradation of pentachlorophenol.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/19325743"/>
<citation rdf:resource="http://purl.uniprot.org/citations/23676275"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.404#SIP7FADEB4269B7EA44">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>2,3,5,6-tetrachlorohydroquinone + H(+) + NAD(+) = 2,3,5,6-tetrachloro-1,4-benzoquinone + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/19325743">
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/23676275">
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.405">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>ribitol-5-phosphate 2-dehydrogenase (NADP(+))</skos:prefLabel>
<skos:altLabel>D-ribulose 5-phosphate reductase</skos:altLabel>
<skos:altLabel>ribulose-5-phosphate reductase</skos:altLabel>
<skos:altLabel>ribulose-5-P reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.405#SIPAF3C466C85A3061A"/>
<rdfs:comment>The enzyme, characterized in bacteria, is specific for NADP.</rdfs:comment>
<rdfs:comment>It is part of the synthesis pathway of CDP-ribitol.</rdfs:comment>
<rdfs:comment>In Haemophilus influenzae it is part of a multifunctional enzyme also catalyzing EC 2.7.7.40.</rdfs:comment>
<rdfs:comment>Cf. EC 1.1.1.137.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/11305920"/>
<citation rdf:resource="http://purl.uniprot.org/citations/15362865"/>
<citation rdf:resource="http://purl.uniprot.org/citations/18556787"/>
<citation rdf:resource="http://purl.uniprot.org/citations/19074383"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.405#SIPAF3C466C85A3061A">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-ribitol 5-phosphate + NADP(+) = D-ribulose 5-phosphate + H(+) + NADPH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/citations/19074383">
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<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/19074383"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.406">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>galactitol 2-dehydrogenase (L-tagatose-forming)</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.406#SIP67C2134BE39CA145"/>
<rdfs:comment>The enzyme, characterized in the bacterium Rhodobacter sphaeroides has a wide substrate specificity.</rdfs:comment>
<rdfs:comment>In addition to galactitol, it primarily oxidizes D-threitol and xylitol, and in addition to L-tagatose, it primarily reduces L-erythrulose, D-ribulose and L-glyceraldehyde.</rdfs:comment>
<rdfs:comment>It is specific for NAD(+).</rdfs:comment>
<rdfs:comment>The enzyme does show activity with D-tagatose (cf. EC 1.1.1.16).</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/7551050"/>
<citation rdf:resource="http://purl.uniprot.org/citations/20410293"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.406#SIP67C2134BE39CA145">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>galactitol + NAD(+) = H(+) + keto-L-tagatose + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/7551050">
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.407">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>D-altritol 5-dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.407#SIP3AF6091F22248EA8"/>
<rdfs:comment>The enzyme, characterized in Agrobacterium fabrum C58, also has low activity with D-mannitol and D-arabitol.</rdfs:comment>
<rdfs:comment>It is part of a D-altritol degradation pathway.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/26472925"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.407#SIP3AF6091F22248EA8">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-altritol + NAD(+) = H(+) + keto-D-tagatose + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/26472925">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.408">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>4-phospho-D-threonate 3-dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.408#SIPC0365950E14DB633"/>
<rdfs:comment>The enzyme, characterized from bacteria, is involved in a pathway for D-threonate catabolism.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/27402745"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.408#SIPC0365950E14DB633">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>4-O-phospho-D-threonate + NAD(+) = CO2 + dihydroxyacetone phosphate + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/27402745">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/27402745"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.409">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>4-phospho-D-erythronate 3-dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.409#SIP984FD59C6EE1292E"/>
<rdfs:comment>The enzyme, characterized from bacteria, is involved in a pathway for D-erythronate catabolism.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/27402745"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.409#SIP984FD59C6EE1292E">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>4-phospho-D-erythronate + NAD(+) = CO2 + dihydroxyacetone phosphate + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/27402745">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/27402745"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/27402745"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.410">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>D-erythronate 2-dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.410#SIP4F8E4D850277D0B0"/>
<rdfs:comment>The enzyme, characterized from bacteria, is involved in D-erythronate catabolism.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/27402745"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.410#SIP4F8E4D850277D0B0">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-erythronate + NAD(+) = 2-dehydro-D-erythronate + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/27402745">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/27402745"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/27402745"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.411">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>L-threonate 2-dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.411#SIP106498E17F74E165"/>
<rdfs:comment>The enzyme, characterized from bacteria, is involved in L-threonate catabolism.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/27402745"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.411#SIP106498E17F74E165">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>L-threonate + NAD(+) = 2-dehydro-L-erythronate + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/27402745">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/27402745"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/27402745"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.412">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>2-alkyl-3-oxoalkanoate reductase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.412#SIPB5A8243B1071ACC0"/>
<rdfs:comment>The enzyme, found in certain bacterial species, is part of a pathway for the production of olefins.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/21958090"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.412#SIPB5A8243B1071ACC0">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>a (2R,3S)-2-alkyl-3-hydroxyalkanoate + NADP(+) = an (R)-2-alkyl-3-oxoalkanoate + H(+) + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/21958090">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/21958090"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/21958090"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.413">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>A-factor type gamma-butyrolactone 1'-reductase (1S-forming)</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.413#SIPBBF6F4408E4C066E"/>
<rdfs:comment>The enzyme, which is found in bacteria that produce virginiae-butanolide (VB) type gamma-butyrolactone autoregulators, reduces its substrate stereospecifically, forming a hydroxyl group in the (S) configuration.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/12193632"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.413#SIPBBF6F4408E4C066E">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>a (3R,4R)-3-[(1S)-1-hydroxyalkyl]-4-(hydroxymethyl)oxolan-2-one + NADP(+) = a (3R,4R)-3-alkanoyl-4-(hydroxymethyl)oxolan-2-one + H(+) + NADPH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.414">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>L-galactonate 5-dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.414#SIPD60CBFA256DC0FBB"/>
<rdfs:comment>The enzyme, reported from the human gut bacteria Escherichia coli and Bacteroides vulgatus, participates in an L-galactonate degradation pathway.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/381020"/>
<citation rdf:resource="http://purl.uniprot.org/citations/24861318"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.414#SIPD60CBFA256DC0FBB">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>L-galactonate + NAD(+) = H(+) + keto-D-tagaturonate + NADH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/citations/24963813">
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.415">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>noscapine synthase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.415#SIP7214B7CF2DE435EB"/>
<rdfs:comment>The enzyme, characterized from the plant Papaver somniferum (opium poppy), catalyzes the last step in the biosynthesis of the isoquinoline alkaloid noscapine.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/24708518"/>
<citation rdf:resource="http://purl.uniprot.org/citations/29610307"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.415#SIP7214B7CF2DE435EB">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>NAD(+) + narcotine hemiacetal = H(+) + NADH + noscapine.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/24708518">
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<rdf:Description rdf:about="http://purl.uniprot.org/citations/29610307">
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<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/29610307"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.416">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>isopyridoxal dehydrogenase (5-pyridoxolactone-forming)</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.416#SIP6370CEBAFBA8C15C"/>
<rdfs:comment>The enzyme, characterized from the bacterium Arthrobacter sp Cr-7, participates in the degradation of pyridoxine.</rdfs:comment>
<rdfs:comment>The enzyme also catalyzes the activity of EC 1.2.1.102.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/3533936"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.416#SIP6370CEBAFBA8C15C">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>isopyridoxal + NAD(+) = 5-pyridoxolactone + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/3533936">
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.417">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>3beta-hydroxysteroid-4beta-carboxylate 3-dehydrogenase (decarboxylating)</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.417#SIP4D2BF25CA4E5D2F7"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.417#SIP67A8297AA73B4AE7"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.417#SIP2EA989F7A3C76DAA"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.417#SIP0CE3244121178398"/>
<rdfs:comment>This bacterial enzyme participates in the biosynthesis of bacterial sterols.</rdfs:comment>
<rdfs:comment>Together with EC 1.14.13.246 (SdmA) it forms an enzyme system that removes one methyl group from the C-4 position of 4,4-dimethylated steroid molecules.</rdfs:comment>
<rdfs:comment>SdmA catalyzes three successive oxidations of the C-4beta methyl group, turning it into a carboxylate group; SdmB is a bifunctional enzyme that catalyzes two different activities.</rdfs:comment>
<rdfs:comment>As EC 1.1.1.417 it catalyzes an oxidative decarboxylation that results in reduction of the 3beta-hydroxy group at the C-3 carbon to an oxo group.</rdfs:comment>
<rdfs:comment>As EC 1.1.1.270, it reduces the 3-oxo group back to a 3beta-hydroxyl.</rdfs:comment>
<rdfs:comment>Since the remaining methyl group at C-4 is in an alpha orientation, it cannot serve as a substrate for a second round of demethylation by this system.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/29784781"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.417#SIP4D2BF25CA4E5D2F7">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>a 3beta-hydroxy-4alpha-methylsteroid-4beta-carboxylate + NAD(+) = a 4alpha-methyl-3-oxosteroid + CO2 + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.417#SIP67A8297AA73B4AE7">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>a 3beta-hydroxy-4alpha-methylsteroid-4beta-carboxylate + NADP(+) = a 4alpha-methyl-3-oxosteroid + CO2 + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.417#SIP2EA989F7A3C76DAA">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>4beta-carboxy-4alpha-methyl-5alpha-cholesta-8,24-dien-3beta-ol + NAD(+) = 3-dehydro-4alpha-methylzymosterol + CO2 + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.417#SIP0CE3244121178398">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>4beta-carboxy-4alpha-methyl-5alpha-cholesta-8,24-dien-3beta-ol + NADP(+) = 3-dehydro-4alpha-methylzymosterol + CO2 + NADPH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/29784781">
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<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/29784781"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.418">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>plant 3beta-hydroxysteroid-4alpha-carboxylate 3-dehydrogenase (decarboxylating)</skos:prefLabel>
<skos:altLabel>3beta-hydroxysteroid dehydrogenases/C-4 decarboxylase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.418#SIP6A7D2522E1277DA3"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.418#SIPDA2A6D57FD2367E1"/>
<rdfs:comment>The enzyme, found in plants, catalyzes multiple reactions during plant sterol biosynthesis.</rdfs:comment>
<rdfs:comment>Unlike the fungal/animal enzyme EC 1.1.1.170 the plant enzyme is specific for NAD(+).</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/10356290"/>
<citation rdf:resource="http://purl.uniprot.org/citations/16835224"/>
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<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.418#SIP6A7D2522E1277DA3">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>a 3beta-hydroxysteroid-4alpha-carboxylate + NAD(+) = a 3-oxosteroid + CO2 + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.418#SIPDA2A6D57FD2367E1">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>4alpha-carboxy-4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-ergost-24(24(1))-en-3beta-ol + NAD(+) = CO2 + cycloeucalenone + NADH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/citations/16835224">
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<rdf:Description rdf:about="http://purl.uniprot.org/citations/19218365">
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.419">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>nepetalactol dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.419#SIPBF84374C67157A41"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.419#SIPBF9BE7AD612DECD8"/>
<rdfs:comment>The enzyme, characterized from the plant Nepeta mussinii, binds an NAD(+) cofactor.</rdfs:comment>
<rdfs:comment>It also catalyzes the activity of EC 5.5.1.34.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/30531909"/>
<citation rdf:resource="http://purl.uniprot.org/citations/30664302"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.419#SIPBF84374C67157A41">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>cis-cis-nepetalactol + NAD(+) = cis-cis-nepetalactone + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.419#SIPBF9BE7AD612DECD8">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>cis-trans-nepetalactol + NAD(+) = cis-trans-nepetalactone + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/citations/30664302">
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<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/30664302"/>
<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/30664302"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.420">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>D-apiose dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.420#SIP07DAA6677EA4A4ED"/>
<rdfs:comment>The enzyme, characterized from several bacterial species, is involved in a catabolic pathway for D-apiose.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/29867142"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.420#SIP07DAA6677EA4A4ED">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-apiofuranose + NAD(+) = D-apionolactone + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/29867142">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
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<foaf:primaryTopicOf rdf:resource="https://pubmed.ncbi.nlm.nih.gov/29867142"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.421">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>D-apionate oxidoisomerase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.421#SIPA3644F6F7612C74D"/>
<rdfs:comment>The enzyme, characterized from several bacterial species, participates in the degradation of D-apionate.</rdfs:comment>
<rdfs:comment>The reaction involves migration of a hydroxymethyl group from position 3 to position 2 and oxidation of the 3-hydroxyl group.</rdfs:comment>
<rdfs:comment>Stereospecificity of the product, 3-oxoisoapionate, has not been determined.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/29867142"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.421#SIPA3644F6F7612C74D">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-apionate + NAD(+) = 3-oxoisoapionate + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/29867142">
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.422">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>pseudoephedrine dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.422#SIP4F215BC24CCBA8A2"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.422#SIP19AB400802025DEC"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.422#SIP4C773EDBEFCC1223"/>
<rdfs:comment>The enzyme, characterized from the bacterium Arthrobacter sp. TS-15, acts on a broad range of different aryl-alkyl ketones, such as haloketones, ketoamines, diketones, and ketoesters.</rdfs:comment>
<rdfs:comment>It accepts various types of aryl groups including phenyl-, pyridyl-, thienyl-, and furyl-rings, but the presence of an aromatic ring is essential for the activity.</rdfs:comment>
<rdfs:comment>In addition, the presence of a functional group on the alkyl chain, such as an amine, a halogen, or a ketone, is also crucial.</rdfs:comment>
<rdfs:comment>The enzyme exhibits a strict anti-Prelog enantioselectivity.</rdfs:comment>
<rdfs:comment>When acting on diketones, it catalyzes the reduction of only the keto group closest to the ring, with no further reduction to the diol.</rdfs:comment>
<rdfs:comment>Cf. EC 1.1.1.423.</rdfs:comment>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.422#SIP4F215BC24CCBA8A2">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(1S,2S)-pseudoephedrine + NAD(+) = (S)-2-methylamino-1-phenylpropan-1-one + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.422#SIP19AB400802025DEC">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(1S,2R)-ephedrine + NAD(+) = (R)-2-methylamino-1-phenylpropan-1-one + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.422#SIP4C773EDBEFCC1223">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(S)-phenylacetylcarbinol + NAD(+) = 1-phenyl-1,2-propanedione + H(+) + NADH.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.423">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>(1R,2S)-ephedrine 1-dehydrogenase</skos:prefLabel>
<skos:altLabel>ephedrine dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.423#SIPD45953C9BE7E2383"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.423#SIP40B97965A1B86BA0"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.423#SIPB39D40EB4CD40733"/>
<rdfs:comment>The enzyme, characterized from the bacterium Arthrobacter sp. TS-15, acts on a broad range of different aryl-alkyl ketones, such as haloketones, ketoamines, diketones, and ketoesters.</rdfs:comment>
<rdfs:comment>It exhibits a strict enantioselectivity and accepts various types of aryl groups including phenyl-, pyridyl-, thienyl-, and furyl-rings, but the presence of an aromatic ring is essential for the activity.</rdfs:comment>
<rdfs:comment>In addition, the presence of a functional group on the alkyl chain, such as an amine, a halogen, or a ketone, is also crucial.</rdfs:comment>
<rdfs:comment>When acting on diketones, it catalyzes the reduction of only the keto group closest to the ring, with no further reduction to the diol.</rdfs:comment>
<rdfs:comment>Cf. EC 1.1.1.422 and EC 1.5.1.18.</rdfs:comment>
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<rdfs:label>(1R,2S)-ephedrine + NAD(+) = (S)-2-methylamino-1-phenylpropan-1-one + H(+) + NADH.</rdfs:label>
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<rdfs:label>(1R,2R)-pseudoephedrine + NAD(+) = (R)-2-methylamino-1-phenylpropan-1-one + H(+) + NADH.</rdfs:label>
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<rdfs:label>(R)-phenylacetylcarbinol + NAD(+) = 1-phenyl-1,2-propanedione + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>D-xylose 1-dehydrogenase (NADP(+), D-xylono-1,4-lactone-forming)</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.424#SIPD33CC2FB45E6E5FC"/>
<rdfs:comment>The enzyme, which participates in the degradation of D-xylose, has been characterized from several halophilic archaeal species.</rdfs:comment>
<rdfs:comment>Cf. EC 1.1.1.179.</rdfs:comment>
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<rdfs:label>D-xylofuranose + NADP(+) = D-xylono-1,4-lactone + H(+) + NADPH.</rdfs:label>
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<skos:prefLabel>levoglucosan dehydrogenase</skos:prefLabel>
<skos:altLabel>1,6-anhydro-beta-D-glucose dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.425#SIP7075DE9A920986F6"/>
<rdfs:comment>Levoglucosan is formed from the pyrolysis of carbohydrates such as starch and cellulose and is an important molecular marker for pollution from biomass burning.</rdfs:comment>
<rdfs:comment>This enzyme is present only in bacteria, and has been characterized from Arthrobacter sp. I-552 and Pseudarthrobacter phenanthrenivorans.</rdfs:comment>
<rdfs:comment>Cf. EC 2.7.1.232.</rdfs:comment>
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<rdfs:label>levoglucosan + NAD(+) = 3-dehydrolevoglucosan + H(+) + NADH.</rdfs:label>
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<skos:prefLabel>UDP-N-acetyl-alpha-D-quinovosamine dehydrogenase</skos:prefLabel>
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<rdfs:comment>The enzyme participates in the biosynthesis of N-acetyl-alpha-D-quinovosamine, a 6-deoxy sugar that is present in the O antigens of many Gram-negative bacteria, including Pseudomonas aeruginosa serotypes O6 and O10, Rhizobium etli, and Brucella abortus.</rdfs:comment>
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<rdfs:label>NADP(+) + UDP-N-acetyl-alpha-D-quinovosamine = H(+) + NADPH + UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hex-4-ulose.</rdfs:label>
</rdf:Description>
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<rdfs:label>NAD(+) + UDP-N-acetyl-alpha-D-quinovosamine = H(+) + NADH + UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hex-4-ulose.</rdfs:label>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>D-arabinose 1-dehydrogenase (NADP(+))</skos:prefLabel>
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<rdfs:comment>The enzyme from the archaeon Saccharolobus solfataricus is tetrameric and contains zinc.</rdfs:comment>
<rdfs:comment>L-fucose also is a substrate.</rdfs:comment>
<rdfs:comment>In contrast to EC 1.1.1.116 and EC 1.1.1.117, this enzyme is specific for NADP(+).</rdfs:comment>
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<rdfs:label>D-arabinose + NADP(+) = D-arabinono-1,4-lactone + H(+) + NADPH.</rdfs:label>
</rdf:Description>
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<dcterms:identifier>doi:10.1074/jbc.m605549200</dcterms:identifier>
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<dcterms:identifier>doi:10.1016/j.jmb.2007.05.097</dcterms:identifier>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.428">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>4-methylthio 2-oxobutanoate reductase (NADH)</skos:prefLabel>
<skos:altLabel>4-methylthio 2-oxobutyrate reductase</skos:altLabel>
<skos:altLabel>4-methylthio 2-oxobutyric acid reductase</skos:altLabel>
<skos:altLabel>MTOB reductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.428#SIPB57C62C59333694B"/>
<rdfs:comment>The substrate of this enzyme is formed as an intermediate during L-methionine salvage from S-methyl-5'-thioadenosine, which is formed during the biosynthesis of polyamines.</rdfs:comment>
<rdfs:comment>The human enzyme also functions as a transcriptional co-regulator that downregulates the expression of many tumor-suppressor genes, thus providing a link between gene repression and the methionine salvage pathway.</rdfs:comment>
<rdfs:comment>A similar, but NADP-specific, enzyme is involved in dimethylsulfoniopropanoate biosynthesis in algae and phytoplankton.</rdfs:comment>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(2R)-2-hydroxy-4-(methylsulfanyl)butanoate + NAD(+) = 4-methylsulfanyl-2-oxobutanoate + H(+) + NADH.</rdfs:label>
</rdf:Description>
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<dcterms:identifier>doi:10.1016/s1097-2765(02)00650-0</dcterms:identifier>
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<dcterms:identifier>doi:10.1016/j.bbrc.2006.11.111</dcterms:identifier>
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<dcterms:identifier>doi:10.1016/j.febslet.2014.03.026</dcterms:identifier>
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<dcterms:identifier>doi:10.1016/j.bmc.2016.04.037</dcterms:identifier>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.429">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>(2S)-[(R)-hydroxy(phenyl)methyl]succinyl-CoA dehydrogenase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.1.429#SIP01EFCC06E1B2D3DF"/>
<rdfs:comment>The enzyme, purified from the bacterium Thauera aromatica, is involved in an anaerobic toluene degradation pathway.</rdfs:comment>
<rdfs:comment>It is specific for NAD(+).</rdfs:comment>
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<rdfs:label>(2S)-[(R)-hydroxy(phenyl)methyl]succinyl-CoA + NAD(+) = (S)-2-benzoylsuccinyl-CoA + H(+) + NADH.</rdfs:label>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.n1">
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<obsolete rdf:datatype="http://www.w3.org/2001/XMLSchema#boolean">true</obsolete>
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<obsolete rdf:datatype="http://www.w3.org/2001/XMLSchema#boolean">true</obsolete>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.n3">
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<skos:prefLabel>(-)-trans-carveol dehydrogenase</skos:prefLabel>
<skos:altLabel>(4R,6S)-carveol dehydrogenase</skos:altLabel>
<skos:altLabel>carveol dehydrogenase</skos:altLabel>
<skos:altLabel>CDH</skos:altLabel>
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<rdfs:comment>Catalyzes the oxidation of carveol to carvone, with a strong stereoselectivity since it efficiently converts only the (6S)-stereoisomers, of which (-)-(4R,6S)-trans-carveol is the better substrate.</rdfs:comment>
<rdfs:comment>Displays a broad substrate specificity with a preference for substituted cyclohexanols, and does not catalyze the oxidation of primary or short chain aliphatic secondary alcohols.</rdfs:comment>
<rdfs:comment>Is also able, albeit more slowly, to oxidize limonene-1,2-diol into 1-hydroxy-2-oxolimonene.</rdfs:comment>
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<rdfs:label>(1S,5R)-carveol + NAD(+) = (R)-carvone + H(+) + NADH.</rdfs:label>
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<rdfs:label>(1S,5S)-carveol + NAD(+) = (S)-carvone + H(+) + NADH.</rdfs:label>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.1.n5">
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<skos:prefLabel>3-methylmalate dehydrogenase</skos:prefLabel>
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<rdfs:comment>The enzyme from Methanocaldococcus jannaschii also catalyzes the reaction of EC 1.1.1.85 and EC 1.1.1.83.</rdfs:comment>
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<rdfs:label>(2R,3S)-3-methylmalate + NAD(+) = 2-oxobutanoate + CO2 + NADH.</rdfs:label>
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<rdfs:label>4-hydroxybutanoate + NADP(+) = H(+) + NADPH + succinate semialdehyde.</rdfs:label>
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<rdfs:label>a (3R)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH.</rdfs:label>
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<skos:prefLabel>With a cytochrome as acceptor</skos:prefLabel>
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<rdfs:label>D-mannitol + 2 Fe(III)-[cytochrome c] = D-fructose + 2 Fe(II)-[cytochrome c] + 2 H(+).</rdfs:label>
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<skos:prefLabel>L-lactate dehydrogenase (cytochrome)</skos:prefLabel>
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<skos:altLabel>lactic acid dehydrogenase</skos:altLabel>
<skos:altLabel>L-lactate ferricytochrome c oxidoreductase</skos:altLabel>
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<rdfs:label>(S)-lactate + 2 Fe(III)-[cytochrome c] = 2 Fe(II)-[cytochrome c] + 2 H(+) + pyruvate.</rdfs:label>
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<skos:prefLabel>D-lactate dehydrogenase (cytochrome)</skos:prefLabel>
<skos:altLabel>D-lactate ferricytochrome c oxidoreductase</skos:altLabel>
<skos:altLabel>lactic acid dehydrogenase</skos:altLabel>
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<rdfs:label>(R)-lactate + 2 Fe(III)-[cytochrome c] = 2 Fe(II)-[cytochrome c] + 2 H(+) + pyruvate.</rdfs:label>
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<rdfs:comment>The enzyme from the sulfate-reducing bacterium Desulfovibrio vulgaris can also act on (R)-2-hydroxybutanoate.</rdfs:comment>
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<rdfs:label>(R)-lactate + 2 Fe(III)-[cytochrome c553] = 2 Fe(II)-[cytochrome c553] + 2 H(+) + pyruvate.</rdfs:label>
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<skos:prefLabel>polyvinyl alcohol dehydrogenase (cytochrome)</skos:prefLabel>
<skos:altLabel>PVA dehydrogenase</skos:altLabel>
<skos:altLabel>PVADH</skos:altLabel>
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<rdfs:comment>The enzyme is involved in bacterial polyvinyl alcohol degradation.</rdfs:comment>
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<rdfs:label>a polyvinyl alcohol + 2n Fe(III)-[cytochrome c] = an oxidized polyvinyl alcohol + 2n Fe(II)-[cytochrome c] + 2n H(+).</rdfs:label>
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<skos:prefLabel>methanol dehydrogenase (cytochrome c)</skos:prefLabel>
<skos:altLabel>MDH</skos:altLabel>
<skos:altLabel>methanol dehydrogenase</skos:altLabel>
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<rdfs:comment>A periplasmic quinoprotein alcohol dehydrogenase that only occurs in methylotrophic bacteria.</rdfs:comment>
<rdfs:comment>It uses the novel specific cytochrome cL as acceptor.</rdfs:comment>
<rdfs:comment>Acts on a wide range of primary alcohols, including ethanol, duodecanol, chloroethanol, cinnamyl alcohol, and also formaldehyde.</rdfs:comment>
<rdfs:comment>Activity is stimulated by ammonia or methylamine.</rdfs:comment>
<rdfs:comment>It is usually assayed with phenazine methosulfate.</rdfs:comment>
<rdfs:comment>Like all other quinoprotein alcohol dehydrogenases it has an 8-bladed 'propeller' structure, a calcium ion bound to the PQQ in the active site and an unusual disulfide ring structure in close proximity to the PQQ.</rdfs:comment>
<rdfs:comment>It differs from EC 1.1.2.8, alcohol dehydrogenase (cytochrome c), in having a high affinity for methanol and in having a second essential small subunit (no known function).</rdfs:comment>
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<skos:altLabel>BDH</skos:altLabel>
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<rdfs:comment>This periplasmic quinoprotein alcohol dehydrogenase, characterized from the bacterium Thauera butanivorans, is involved in butane degradation.</rdfs:comment>
<rdfs:comment>It contains both pyrroloquinoline quinone (PQQ) and heme c prosthetic groups.</rdfs:comment>
<rdfs:comment>Cf. EC 1.1.5.11.</rdfs:comment>
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<rdfs:label>butan-1-ol + 2 Fe(III)-[cytochrome c] = butanal + 2 Fe(II)-[cytochrome c] + 2 H(+).</rdfs:label>
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<skos:prefLabel>lanthanide-dependent methanol dehydrogenase</skos:prefLabel>
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<skos:altLabel>cerium dependent MDH</skos:altLabel>
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<rdfs:comment>The higher lanthanides show decreasing activity with Sm(3+), Eu(3+) and Gd(3+).</rdfs:comment>
<rdfs:comment>The lanthanide is coordinated by the enzyme and pyrroloquinoline quinone.</rdfs:comment>
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<rdfs:label>2 Fe(III)-[cytochrome cL] + methanol = 2 Fe(II)-[cytochrome cL] + formaldehyde + 2 H(+).</rdfs:label>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.4#SIP9FD10AC62AD02B36">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>beta-D-glucose + O2 = D-glucono-1,5-lactone + H2O2.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.5">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>hexose oxidase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.5#SIP9FD10AC62AD02B36"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.5#SIPDB26939CC2746477"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.5#SIP63FB199F555BDD49"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.5#SIP2485812C9C7F49EA"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.5#SIPF9039F29ABA1FA89"/>
<rdfs:comment>Also oxidizes D-galactose, D-mannose, maltose, lactose and cellobiose.</rdfs:comment>
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<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.5#SIP9FD10AC62AD02B36">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>beta-D-glucose + O2 = D-glucono-1,5-lactone + H2O2.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.5#SIPDB26939CC2746477">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-galactose + O2 = D-galactono-1,5-lactone + H2O2.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.5#SIP63FB199F555BDD49">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-cellobiose + O2 = D-cellobiono-1,5-lactone + H2O2.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.5#SIP2485812C9C7F49EA">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-maltose + O2 = D-maltobiono-1,5-lactone + H2O2.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.5#SIPF9039F29ABA1FA89">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>beta-lactose + O2 = H2O2 + lactobiono-1,5-lactone.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.6">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>cholesterol oxidase</skos:prefLabel>
<skos:altLabel>cholesterol-O2 oxidoreductase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.6#SIPEF26255B10307188"/>
<rdfs:comment>Cholesterol oxidases are secreted bacterial bifunctional enzymes that catalyze the first two steps in the degradation of cholesterol.</rdfs:comment>
<rdfs:comment>The enzyme catalyzes the oxidation of the 3beta-hydroxyl group to a keto group, and the isomerization of the double bond in the oxidized steroid ring system from the Delta(5) position to the Delta(6) position (cf. EC 5.3.3.1).</rdfs:comment>
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<citation rdf:resource="http://purl.uniprot.org/citations/10822008"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.6#SIPEF26255B10307188">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>cholesterol + O2 = cholest-5-en-3-one + H2O2.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.7">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>aryl-alcohol oxidase</skos:prefLabel>
<skos:altLabel>veratryl alcohol oxidase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.7#SIP608E8ACA5DCA986A"/>
<rdfs:comment>Oxidizes many primary alcohols containing an aromatic ring; best substrates are (2-naphthyl)methanol and 3-methoxybenzyl alcohol.</rdfs:comment>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.7#SIP608E8ACA5DCA986A">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.8">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>L-gulonolactone oxidase</skos:prefLabel>
<skos:altLabel>GLO</skos:altLabel>
<skos:altLabel>L-gulono-gamma-lactone oxidase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.8#SIP3D8E8BB24BD73706"/>
<rdfs:comment>The product spontaneously isomerizes to L-ascorbate.</rdfs:comment>
<rdfs:comment>While most higher animals can synthesize ascorbic acid, primates and guinea pigs cannot.</rdfs:comment>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.8#SIP3D8E8BB24BD73706">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>L-gulono-1,4-lactone + O2 = H(+) + H2O2 + L-ascorbate.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.9">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>galactose oxidase</skos:prefLabel>
<skos:altLabel>beta-galactose oxidase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.9#SIP002C84F400CCAD36"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.-"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.9#SIP002C84F400CCAD36">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-galactose + O2 = D-galacto-hexodialdose + H2O2.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.10">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>pyranose oxidase</skos:prefLabel>
<skos:altLabel>glucose 2-oxidase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.10#SIP751A1E66F69D253C"/>
<rdfs:comment>Also oxidizes D-xylose, L-sorbose and D-glucono-1,5-lactone, which have the same ring conformation and configuration at C-2, C-3 and C-4.</rdfs:comment>
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<citation rdf:resource="http://purl.uniprot.org/citations/5725162"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.10#SIP751A1E66F69D253C">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-glucose + O2 = 2-dehydro-D-glucose + H2O2.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/5722278">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/5722278"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/5725162">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Citation"/>
<skos:exactMatch rdf:resource="http://purl.uniprot.org/pubmed/5725162"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.11">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>L-sorbose oxidase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.11#SIPDFA6DB01A79A0625"/>
<rdfs:comment>Also acts on D-glucose, D-galactose and D-xylose, but not on D-fructose.</rdfs:comment>
<rdfs:comment>2,6-dichloroindophenol can act as acceptor.</rdfs:comment>
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<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.11#SIPDFA6DB01A79A0625">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>keto-L-sorbose + O2 = 5-dehydro-D-fructose + H2O2.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.12">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>pyridoxine 4-oxidase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.12#SIP0960303CC8F06E76"/>
<rdfs:comment>2,6-dichloroindophenol can act as acceptor.</rdfs:comment>
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<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.12#SIP0960303CC8F06E76">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>O2 + pyridoxine = H2O2 + pyridoxal.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.13">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>alcohol oxidase</skos:prefLabel>
<skos:altLabel>AOX</skos:altLabel>
<skos:altLabel>methanol oxidase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.13#SIP8F54D1A547BBBE47"/>
<rdfs:comment>The enzymes from the fungi Candida methanosorbosa and several Basidiomycetes species contain an FAD cofactor.</rdfs:comment>
<rdfs:comment>The enzyme from the phytopathogenic fungi Colletotrichum graminicola and Colletotrichum gloeosporioides utilize a mononuclear copper-radical mechanism.</rdfs:comment>
<rdfs:comment>The enzyme acts on primary alcohols and unsaturated alcohols, and has much lower activity with branched-chain and secondary alcohols.</rdfs:comment>
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<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.13#SIP8F54D1A547BBBE47">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>a primary alcohol + O2 = an aldehyde + H2O2.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.14">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>catechol oxidase (dimerizing)</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.14#SIP0A3B3AE13039D5C4"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.14#SIP0A3B3AE13039D5C4">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>4 catechol + 3 O2 = 2 dibenzo[1,4]dioxin-2,3-dione + 6 H2O.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.15">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<replaces rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.1"/>
<skos:prefLabel>(S)-2-hydroxy-acid oxidase</skos:prefLabel>
<skos:altLabel>glycolate oxidase</skos:altLabel>
<skos:altLabel>hydroxy-acid oxidase A</skos:altLabel>
<skos:altLabel>hydroxy-acid oxidase B</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.15#SIP7EA4B27C6CB73437"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.15#SIPC147DEC4CB142A2F"/>
<rdfs:comment>Exists as two major isoenzymes; the A form preferentially oxidizes short-chain aliphatic hydroxy acids; the B form preferentially oxidizes long-chain and aromatic hydroxy acids.</rdfs:comment>
<rdfs:comment>The rat isoenzyme B also acts as EC 1.4.3.2.</rdfs:comment>
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<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.15#SIP7EA4B27C6CB73437">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>a (2S)-2-hydroxycarboxylate + O2 = a 2-oxocarboxylate + H2O2.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.15#SIPC147DEC4CB142A2F">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>glycolate + O2 = glyoxylate + H2O2.</rdfs:label>
</rdf:Description>
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<skos:prefLabel>ecdysone oxidase</skos:prefLabel>
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<rdfs:comment>2,6-dichloroindophenol can act as acceptor.</rdfs:comment>
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<rdfs:label>ecdysone + O2 = 3-dehydroecdysone + H2O2.</rdfs:label>
</rdf:Description>
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<skos:prefLabel>choline oxidase</skos:prefLabel>
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<rdfs:comment>In many bacteria, plants and animals, the osmoprotectant betaine is synthesized using different enzymes to catalyze the conversion of (1) choline into betaine aldehyde and (2) betaine aldehyde into betaine.</rdfs:comment>
<rdfs:comment>In plants, the first reaction is catalyzed by EC 1.14.15.7, whereas in animals and many bacteria, it is catalyzed by either EC 1.1.99.1 or EC 1.1.3.17.</rdfs:comment>
<rdfs:comment>The enzyme involved in the second step, EC 1.2.1.8, appears to be the same in those plants, animals and bacteria that use two separate enzymes.</rdfs:comment>
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<rdfs:label>choline + H2O + 2 O2 = glycine betaine + H(+) + 2 H2O2.</rdfs:label>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.18">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>secondary-alcohol oxidase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.18#SIP747DD0471EC447A7"/>
<rdfs:comment>Acts on secondary alcohols with five or more carbons, and polyvinyl alcohols with molecular mass over 300 Da.</rdfs:comment>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.18#SIP747DD0471EC447A7">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>a secondary alcohol + O2 = a ketone + H2O2.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.19">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>4-hydroxymandelate oxidase (decarboxylating)</skos:prefLabel>
<skos:altLabel>4-hydroxymandelate oxidase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.19#SIP13AFE40044E36722"/>
<rdfs:comment>The enzyme from the bacterium Pseudomonas putida is involved in the degradation of mandelate.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/976259"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.19#SIP13AFE40044E36722">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(S)-4-hydroxymandelate + H(+) + O2 = 4-hydroxybenzaldehyde + CO2 + H2O2.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.20">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>long-chain-alcohol oxidase</skos:prefLabel>
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<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.20#SIP34626BDB09182DAB"/>
<rdfs:comment>Oxidizes long-chain fatty alcohols; best substrate is dodecyl alcohol.</rdfs:comment>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.20#SIPB0F26AD6C8BDB61B">
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<rdfs:label>a long-chain primary fatty alcohol + O2 = a long-chain fatty aldehyde + H2O2.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.20#SIP34626BDB09182DAB">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>dodecan-1-ol + O2 = dodecanal + H2O2.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.21">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>glycerol-3-phosphate oxidase</skos:prefLabel>
<skos:altLabel>alpha-glycerophosphate oxidase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.21#SIP2B7ACFA0FD27B6C6"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.21#SIP2B7ACFA0FD27B6C6">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>O2 + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H2O2.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.22">
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<obsolete rdf:datatype="http://www.w3.org/2001/XMLSchema#boolean">true</obsolete>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.23">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>thiamine oxidase</skos:prefLabel>
<skos:altLabel>thiamine dehydrogenase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.23#SIP4223DBEAFB6D23CB"/>
<rdfs:comment>The product differs from thiamine in replacement of -CH2-CH2-OH by -CH2-COOH; the two-step oxidation proceeds without the release of the intermediate aldehyde from the enzyme.</rdfs:comment>
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<rdfs:label>H2O + 2 O2 + thiamine = H(+) + 2 H2O2 + thiamine acetate.</rdfs:label>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.25">
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.26">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.27">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>hydroxyphytanate oxidase</skos:prefLabel>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>(2S)-2-hydroxyphytanate + O2 = 2-oxophytanate + H2O2.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.28">
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<skos:prefLabel>nucleoside oxidase</skos:prefLabel>
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<rdfs:comment>Other purine and pyrimidine nucleosides (as well as 2'-deoxyribonucleosides) are substrates, but ribose and nucleotides are not substrates.</rdfs:comment>
<rdfs:comment>The overall reaction takes place in two separate steps, with the 5'-dehydro nucleoside being released from the enzyme to serve as substrate for the second reaction.</rdfs:comment>
<rdfs:comment>Differs from EC 1.1.3.39 as it produces water rather than hydrogen peroxide.</rdfs:comment>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.28#SIP1C8D29FEE74A338F">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>inosine + O2 = 9-riburonosylhypoxanthine + H(+) + H2O.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.29">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>N-acylhexosamine oxidase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.29#SIP1F7EEF40413C27F4"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.29#SIP1D746147A6A1DF27"/>
<rdfs:comment>The enzyme, found in bacteria, also acts more slowly on N-acetyl-D-mannosamine.</rdfs:comment>
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<citation rdf:resource="http://purl.uniprot.org/citations/SIPA92E437F3CD7880E"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.29#SIP1F7EEF40413C27F4">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>H2O + N-acetyl-D-glucosamine + O2 = H(+) + H2O2 + N-acetyl-D-glucosaminate.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.29#SIP1D746147A6A1DF27">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>H2O + N-acetyl-D-galactosamine + O2 = H(+) + H2O2 + N-acetyl-D-galactosaminate.</rdfs:label>
</rdf:Description>
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<dcterms:identifier>doi:10.1080/00021369.1989.10869298</dcterms:identifier>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.30">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>polyvinyl-alcohol oxidase</skos:prefLabel>
<skos:altLabel>PVA oxidase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.30#SIPA3FC28F240C8AA8A"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.-"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.30#SIPA3FC28F240C8AA8A">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>a polyvinyl alcohol + n O2 = an oxidized polyvinyl alcohol + n H2O2.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.31">
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<obsolete rdf:datatype="http://www.w3.org/2001/XMLSchema#boolean">true</obsolete>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.32">
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<obsolete rdf:datatype="http://www.w3.org/2001/XMLSchema#boolean">true</obsolete>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.33">
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<obsolete rdf:datatype="http://www.w3.org/2001/XMLSchema#boolean">true</obsolete>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.34">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<obsolete rdf:datatype="http://www.w3.org/2001/XMLSchema#boolean">true</obsolete>
<replacedBy rdf:resource="http://purl.uniprot.org/enzyme/1.14.19.66"/>
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<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.35">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<obsolete rdf:datatype="http://www.w3.org/2001/XMLSchema#boolean">true</obsolete>
<replacedBy rdf:resource="http://purl.uniprot.org/enzyme/1.14.19.67"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.36">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<obsolete rdf:datatype="http://www.w3.org/2001/XMLSchema#boolean">true</obsolete>
<replacedBy rdf:resource="http://purl.uniprot.org/enzyme/1.14.19.68"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.37">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>D-arabinono-1,4-lactone oxidase</skos:prefLabel>
<skos:altLabel>D-arabinono-gamma-lactone oxidase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.37#SIPC94B150F59431476"/>
<citation rdf:resource="http://purl.uniprot.org/citations/7957197"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.37#SIPC94B150F59431476">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-arabinono-1,4-lactone + O2 = dehydro-D-arabinono-1,4-lactone + H(+) + H2O2.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/7957197">
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.38">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>vanillyl-alcohol oxidase</skos:prefLabel>
<skos:altLabel>4-hydroxy-2-methoxybenzyl alcohol oxidase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.38#SIP47445E3A1DE8FF56"/>
<rdfs:comment>Converts a wide range of 4-hydroxybenzyl alcohols and 4-hydroxybenzylamines into the corresponding aldehydes.</rdfs:comment>
<rdfs:comment>The allyl group of 4-allylphenols is also converted into the -CH=CH-CH2OH group.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/1396672"/>
<citation rdf:resource="http://purl.uniprot.org/citations/8529652"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.-"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.38#SIP47445E3A1DE8FF56">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>4-hydroxy-3-methoxy-benzenemethanol + O2 = H2O2 + vanillin.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.39">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>nucleoside oxidase (H2O2-forming)</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.39#SIP9A88AADEAA34E819"/>
<rdfs:comment>Other purine and pyrimidine nucleosides (as well as 2'-deoxyribonucleosides and arabinosides) are substrates, but ribose and nucleotides are not substrates.</rdfs:comment>
<rdfs:comment>The 5'-dehydro nucleoside is being released from the enzyme to serve as substrate for the second reaction.</rdfs:comment>
<rdfs:comment>Differs from EC 1.1.3.28 as it produces hydrogen peroxide rather than water.</rdfs:comment>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.39#SIP9A88AADEAA34E819">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>adenosine + H2O + 2 O2 = 9-riburonosyladenine + H(+) + 2 H2O2.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.40">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>D-mannitol oxidase</skos:prefLabel>
<skos:altLabel>D-arabinitol oxidase</skos:altLabel>
<skos:altLabel>D-arabitol oxidase</skos:altLabel>
<skos:altLabel>mannitol oxidase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.40#SIPA46C71ED4CC20FCD"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.40#SIPEC152324F2093836"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.40#SIPCFE570F100B7C185"/>
<rdfs:comment>Also catalyzes the oxidation of D-arabinitol and, to a lesser extent, D-glucitol (sorbitol), whereas L-arabinitol is not a good substrate.</rdfs:comment>
<rdfs:comment>The enzyme from the snails Helix aspersa and Arion ater is found in a specialized tubular organelle that has been termed the mannosome.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/3519307"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.-"/>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.40#SIPA46C71ED4CC20FCD">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-mannitol + O2 = D-mannose + H2O2.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.40#SIPEC152324F2093836">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-sorbitol + O2 = D-sorbopyranose + H2O2.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.40#SIPCFE570F100B7C185">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>D-arabinitol + O2 = D-arabinose + H2O2.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/citations/3519307">
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.41">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>alditol oxidase</skos:prefLabel>
<skos:altLabel>xylitol oxidase</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.41#SIPF35D53800BA18B51"/>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.41#SIPA826F759755A33B4"/>
<rdfs:comment>While xylitol (five carbons) and sorbitol (6 carbons) are the preferred substrates, other alditols, including L-threitol (four carbons), D-arabinitol (five carbons), D-galactitol (six carbons) and D-mannitol (six carbons) can also act as substrates, but more slowly.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/16232758"/>
<citation rdf:resource="http://purl.uniprot.org/citations/17517896"/>
<citation rdf:resource="http://purl.uniprot.org/citations/18154360"/>
<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.-"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.41#SIPF35D53800BA18B51">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>an alditol + O2 = an aldose + H2O2.</rdfs:label>
</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.41#SIPA826F759755A33B4">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>O2 + xylitol = D-xylose + H2O2.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.42">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>prosolanapyrone-II oxidase</skos:prefLabel>
<skos:altLabel>prosolanapyrone II oxidase/prosolanapyrone III cycloisomerase</skos:altLabel>
<skos:altLabel>Sol5</skos:altLabel>
<skos:altLabel>SPS</skos:altLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.42#SIPB4F425E07C234016"/>
<rdfs:comment>The enzyme is involved in the biosynthesis of the phytotoxin solanapyrone by some fungi.</rdfs:comment>
<rdfs:comment>The bifunctional enzyme catalyzes the oxidation of prosolanapyrone II and the subsequent Diels Alder cycloisomerization of the product prosolanapyrone III to (-)-solanapyrone A (cf. EC 5.5.1.20).</rdfs:comment>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>O2 + prosolanapyrone II = H2O2 + prosolanapyrone III.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.43">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>paromamine 6'-oxidase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.43#SIP6A0631230407A533"/>
<rdfs:comment>Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin.</rdfs:comment>
<rdfs:comment>Works in combination with EC 2.6.1.93 to replace the 6-hydroxy group of paromamine with an amino group.</rdfs:comment>
<rdfs:comment>The enzyme from the bacterium Streptomyces fradiae also catalyzes EC 1.1.3.44.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/17206729"/>
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<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.-"/>
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</rdf:Description>
<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.43#SIP6A0631230407A533">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>O2 + paromamine = 6'-oxoparomamine + H2O2.</rdfs:label>
</rdf:Description>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.44">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>6'''-hydroxyneomycin C oxidase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.44#SIPF9BFA253F22DD2CE"/>
<rdfs:comment>Involved in the biosynthetic pathway of aminoglycoside antibiotics of the neomycin family.</rdfs:comment>
<rdfs:comment>Works in combination with EC 2.6.1.95 to replace the 6'''-hydroxy group of 6'''-hydroxyneomycin C with an amino group.</rdfs:comment>
<rdfs:comment>Also catalyzes EC 1.1.3.43.</rdfs:comment>
<citation rdf:resource="http://purl.uniprot.org/citations/17206729"/>
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<rdfs:subClassOf rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.-"/>
<skos:broaderTransitive rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.-"/>
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<rdf:Description rdf:about="http://purl.uniprot.org/enzyme/1.1.3.44#SIPF9BFA253F22DD2CE">
<rdf:type rdf:resource="http://purl.uniprot.org/core/Catalytic_Activity"/>
<rdfs:label>6'''-deamino-6'''-hydroxyneomycin C + O2 = 6'''-deamino-6'''-oxoneomycin C + H2O2.</rdfs:label>
</rdf:Description>
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<skos:prefLabel>aclacinomycin-N oxidase</skos:prefLabel>
<skos:altLabel>aclacinomycin oxidoreductase</skos:altLabel>
<skos:altLabel>AknOx</skos:altLabel>
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<rdfs:comment>This bifunctional enzyme is a secreted flavin-dependent enzyme that is involved in the modification of the terminal sugar residues in the biosynthesis of aclacinomycins.</rdfs:comment>
<rdfs:comment>The enzyme utilizes the same active site to catalyze the oxidation of the rhodinose moiety of aclacinomycin N to the cinerulose A moiety of aclacinomycin A and the oxidation of the latter to the L-aculose moiety of aclacinomycin Y (cf. EC 1.3.3.14).</rdfs:comment>
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<rdfs:label>aclacinomycin N + O2 = aclacinomycin A + H2O2.</rdfs:label>
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<skos:prefLabel>4-hydroxymandelate oxidase</skos:prefLabel>
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<rdfs:comment>The enzyme from the bacterium Amycolatopsis orientalis is involved in the biosynthesis of L-(4-hydroxyphenyl)glycine and L-(3,5-dihydroxyphenyl)glycine, two non-proteinogenic amino acids occurring in the vancomycin group of antibiotics.</rdfs:comment>
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<rdfs:label>(S)-4-hydroxymandelate + O2 = 4-hydroxyphenylglyoxylate + H2O2.</rdfs:label>
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<skos:prefLabel>5-(hydroxymethyl)furfural oxidase</skos:prefLabel>
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<rdfs:comment>The enzyme, characterized from the bacterium Methylovorus sp. strain MP688, is involved in the degradation and detoxification of 5-(hydroxymethyl)furfural.</rdfs:comment>
<rdfs:comment>The enzyme acts only on alcohol groups and requires the spontaneous hydration of aldehyde groups for their oxidation.</rdfs:comment>
<rdfs:comment>The enzyme has a broad substrate range that overlaps with EC 1.1.3.7.</rdfs:comment>
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<rdfs:label>5-hydroxymethylfurfural + 2 H2O + 3 O2 = 2,5-dicarboxyfuran + 2 H(+) + 3 H2O2.</rdfs:label>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
<skos:prefLabel>3-deoxy-alpha-D-manno-octulosonate 8-oxidase</skos:prefLabel>
<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.3.48#SIPA64B5799E9BD08C4"/>
<rdfs:comment>The enzyme, characterized from the bacterium Shewanella oneidensis, is involved in the formation of 8-amino-3,8-dideoxy-alpha-D-manno-octulosonate, an aminated form of Kdo found in lipopolysaccharides of members of the Shewanella genus.</rdfs:comment>
<rdfs:comment>Cf. EC 2.6.1.109.</rdfs:comment>
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<rdfs:label>3-deoxy-alpha-D-manno-oct-2-ulosonate + O2 = 3,8-dideoxy-8-oxo-alpha-D-manno-octulosonate + H2O2.</rdfs:label>
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<skos:prefLabel>(R)-mandelonitrile oxidase</skos:prefLabel>
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<rdfs:comment>The enzyme, characterized from the millipede Chamberlinius hualienensis, is segregated from its substrate, which is contained in special sacs.</rdfs:comment>
<rdfs:comment>The sacs are ruptured during defensive behavior, allowing the enzyme and substrate to mix in special reaction chambers leading to production of the defensive chemical benzoyl cyanide.</rdfs:comment>
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<rdfs:label>(R)-mandelonitrile + O2 = benzoyl cyanide + H2O2.</rdfs:label>
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<skos:prefLabel>With a disulfide as acceptor</skos:prefLabel>
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<obsolete rdf:datatype="http://www.w3.org/2001/XMLSchema#boolean">true</obsolete>
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<skos:prefLabel>With a quinone or similar compound as acceptor</skos:prefLabel>
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<skos:prefLabel>quinoprotein glucose dehydrogenase (PQQ, quinone)</skos:prefLabel>
<skos:altLabel>D-glucose:(pyrroloquinoline-quinone) 1-oxidoreductase</skos:altLabel>
<skos:altLabel>glucose dehydrogenase (PQQ-dependent)</skos:altLabel>
<skos:altLabel>glucose dehydrogenase (pyrroloquinoline-quinone)</skos:altLabel>
<skos:altLabel>quinoprotein D-glucose dehydrogenase</skos:altLabel>
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<rdfs:comment>Integral membrane protein containing PQQ as prosthetic group.</rdfs:comment>
<rdfs:comment>It also contains bound ubiquinone and Mg(2+) or Ca(2+).</rdfs:comment>
<rdfs:comment>Electron acceptor is membrane ubiquinone but usually assayed with phenazine methosulfate.</rdfs:comment>
<rdfs:comment>Like in all other quinoprotein alcohol dehydrogenases the catalytic domain has an 8-bladed 'propeller' structure.</rdfs:comment>
<rdfs:comment>It occurs in a wide range of bacteria.</rdfs:comment>
<rdfs:comment>Catalyzes a direct oxidation of the pyranose form of D-glucose to the lactone and thence to D-gluconate in the periplasm.</rdfs:comment>
<rdfs:comment>Oxidizes other monosaccharides including the pyranose forms of pentoses.</rdfs:comment>
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<rdfs:label>a ubiquinone + D-glucose = a ubiquinol + D-glucono-1,5-lactone.</rdfs:label>
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<rdf:type rdf:resource="http://purl.uniprot.org/core/Enzyme"/>
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<skos:prefLabel>glycerol-3-phosphate dehydrogenase</skos:prefLabel>
<skos:altLabel>FAD-dependent glycerol-3-phosphate dehydrogenase</skos:altLabel>
<skos:altLabel>flavin-linked glycerol-3-phosphate dehydrogenase</skos:altLabel>
<skos:altLabel>glycerol-3-phosphate CoQ reductase</skos:altLabel>
<skos:altLabel>glycerophosphate dehydrogenase</skos:altLabel>
<skos:altLabel>L-glycerophosphate dehydrogenase</skos:altLabel>
<skos:altLabel>sn-glycerol-3-phosphate dehydrogenase</skos:altLabel>
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<activity rdf:resource="http://purl.uniprot.org/enzyme/1.1.5.3#SIP0B6551D89E096C8A"/>
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<rdfs:comment>An essential membrane enzyme, functioning at the central junction of glycolysis, respiration and phospholipid biosynthesis.</rdfs:comment>
<rdfs:comment>In bacteria, the enzyme is localized to the cytoplasmic membrane, while in eukaryotes it is tightly bound to the outer surface of the inner mitochondrial membrane.</rdfs:comment>
<rdfs:comment>In eukaryotes, this enzyme, together with the cytosolic enzyme EC 1.1.1.8 forms the glycerol-3-phosphate shuttle by which NADH produced in the cytosol, primarily from glycolysis, can be reoxidized to NAD(+) by the mitochondrial electron-transport chain.</rdfs:comment>
<rdfs:comment>This shuttle plays a critical role in transferring reducing equivalents from cytosolic NADH into the mitochondrial matrix.</rdfs:comment>
<rdfs:comment>Insect flight muscle uses only CoQ10 as the physiological quinone whereas hamster and rat mitochondria use mainly CoQ9.</rdfs:comment>
<rdfs:comment>The enzyme is activated by calcium.</rdfs:comment>
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<rdfs:label>a quinone + sn-glycerol 3-phosphate = a quinol + dihydroxyacetone phosphate.</rdfs:label>
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<rdfs:label>sn-glycerol 3-phosphate + ubiquinone-8 = dihydroxyacetone phosphate + ubiquinol-8.</rdfs:label>
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<skos:prefLabel>malate dehydrogenase (quinone)</skos:prefLabel>
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<rdfs:label>(S)-malate + a quinone = a quinol + oxaloacetate.</rdfs:label>
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<skos:prefLabel>alcohol dehydrogenase (quinone)</skos:prefLabel>
<skos:altLabel>PQQ alcohol dehydrogenase</skos:altLabel>
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<skos:altLabel>PQQ-dependent alcohol dehydrogenase</skos:altLabel>
<skos:altLabel>pyrroloquinoline quinone-dependent alcohol dehydrogenase</skos:altLabel>
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