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http://purl.uniprot.org/enzyme/2.1.1.107http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/2.1.1.107http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/2.1.1.-
http://purl.uniprot.org/enzyme/2.1.1.107http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/2.-.-.-
http://purl.uniprot.org/enzyme/2.1.1.107http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/2.1.-.-
http://purl.uniprot.org/enzyme/2.1.1.107http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/2.1.1.107http://www.w3.org/2000/01/rdf-schema#comment"In Saccharomyces cerevisiae, the last two steps are carried out by a single bifunctional enzyme, Met8p."xsd:string
http://purl.uniprot.org/enzyme/2.1.1.107http://www.w3.org/2000/01/rdf-schema#comment"This enzyme catalyzes two sequential methylation reactions, the first forming precorrin-1 and the second leading to the formation of precorrin-2."xsd:string
http://purl.uniprot.org/enzyme/2.1.1.107http://www.w3.org/2000/01/rdf-schema#comment"Also involved in the biosynthesis of cobalamin."xsd:string
http://purl.uniprot.org/enzyme/2.1.1.107http://www.w3.org/2000/01/rdf-schema#comment"The second step involves an NAD(+)-dependent dehydrogenation to form sirohydrochlorin from precorrin-2 (EC 1.3.1.76) and the third step involves the chelation of Fe(2+) to sirohydrochlorin to form siroheme (EC 4.99.1.4)."xsd:string
http://purl.uniprot.org/enzyme/2.1.1.107http://www.w3.org/2000/01/rdf-schema#comment"In some bacteria, steps 1-3 are catalyzed by a single multifunctional protein called CysG, whereas in Bacillus megaterium, three separate enzymes carry out each of the steps, with SirA being responsible for the above reaction."xsd:string
http://purl.uniprot.org/enzyme/2.1.1.107http://www.w3.org/2000/01/rdf-schema#comment"It is the first of three steps leading to the formation of siroheme from uroporphyrinogen III."xsd:string
http://purl.uniprot.org/enzyme/2.1.1.107http://www.w3.org/2004/02/skos/core#prefLabel"uroporphyrinogen-III C-methyltransferase"xsd:string
http://purl.uniprot.org/enzyme/2.1.1.107http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/2407234
http://purl.uniprot.org/enzyme/2.1.1.107http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/11980703
http://purl.uniprot.org/enzyme/2.1.1.107http://www.w3.org/2004/02/skos/core#altLabel"uroporphyrin-III C-methyltransferase"xsd:string
http://purl.uniprot.org/enzyme/2.1.1.107http://www.w3.org/2004/02/skos/core#altLabel"SUMT"xsd:string
http://purl.uniprot.org/enzyme/2.1.1.107http://www.w3.org/2004/02/skos/core#altLabel"uroporphyrinogen III methylase"xsd:string
http://purl.uniprot.org/enzyme/2.1.1.107http://www.w3.org/2004/02/skos/core#altLabel"uroporphyrinogen-III methylase"xsd:string
http://purl.uniprot.org/enzyme/2.1.1.107http://www.w3.org/2004/02/skos/core#altLabel"uroporphyrinogen-III methyltransferase"xsd:string
http://purl.uniprot.org/enzyme/2.1.1.107http://www.w3.org/2004/02/skos/core#altLabel"S-adenosyl-L-methionine-dependent uroporphyrinogen III methylase"xsd:string
http://purl.uniprot.org/enzyme/2.1.1.107http://www.w3.org/2004/02/skos/core#altLabel"urogen III methylase"xsd:string
http://purl.uniprot.org/enzyme/2.1.1.107http://www.w3.org/2004/02/skos/core#altLabel"uroporphyrinogen methyltransferase"xsd:string
http://purl.uniprot.org/enzyme/2.1.1.107http://www.w3.org/2004/02/skos/core#altLabel"adenosylmethionine-uroporphyrinogen III methyltransferase"xsd:string
http://purl.uniprot.org/enzyme/2.1.1.107http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/2.1.1.107#SIPB782F7060DAF84BE
http://purl.uniprot.org/enzyme/2.1.1.107http://www.w3.org/2004/02/skos/core#broaderTransitivehttp://purl.uniprot.org/enzyme/2.1.1.-