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http://purl.uniprot.org/enzyme/1.17.1.11http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/1.17.1.11http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/1.17.1.11http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.-.-.-
http://purl.uniprot.org/enzyme/1.17.1.11http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.17.-.-
http://purl.uniprot.org/enzyme/1.17.1.11http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.17.1.-
http://purl.uniprot.org/enzyme/1.17.1.11http://www.w3.org/2000/01/rdf-schema#comment"The enzyme complex, isolated from the bacterium Gottschalkia acidurici, couples the reduction of NAD(+) and the reduction of ferredoxin with formate via flavin-based electron bifurcation."xsd:string
http://purl.uniprot.org/enzyme/1.17.1.11http://www.w3.org/2004/02/skos/core#prefLabel"formate dehydrogenase (NAD(+), ferredoxin)"xsd:string
http://purl.uniprot.org/enzyme/1.17.1.11http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/1.17.1.11#SIPC028C66345727275
http://purl.uniprot.org/enzyme/1.17.1.11http://www.w3.org/2004/02/skos/core#broaderTransitivehttp://purl.uniprot.org/enzyme/1.17.1.-
http://purl.uniprot.org/enzyme/1.17.1.11http://www.w3.org/2004/02/skos/core#altLabel"electron-bifurcating formate dehydrogenase"xsd:string
http://purl.uniprot.org/enzyme/1.17.1.11http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/23872566
http://purl.uniprot.org/enzyme/1.17.1.11http://purl.uniprot.org/core/replaceshttp://purl.uniprot.org/enzyme/1.2.1.93
http://rdf.rhea-db.org/46952http://rdf.rhea-db.org/echttp://purl.uniprot.org/enzyme/1.17.1.11
http://purl.uniprot.org/enzyme/1.2.1.93http://purl.uniprot.org/core/replacedByhttp://purl.uniprot.org/enzyme/1.17.1.11
http://purl.uniprot.org/enzyme/1.17.1.-http://www.w3.org/2004/02/skos/core#narrowerTransitivehttp://purl.uniprot.org/enzyme/1.17.1.11