http://purl.uniprot.org/enzyme/2.1.1.107 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/2.1.1.107 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/2.1.1.- |
http://purl.uniprot.org/enzyme/2.1.1.107 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/2.-.-.- |
http://purl.uniprot.org/enzyme/2.1.1.107 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/2.1.-.- |
http://purl.uniprot.org/enzyme/2.1.1.107 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/2.1.1.107 | http://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/2.1.1.107 | http://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/2.1.1.107 | http://www.w3.org/2000/01/rdf-schema#comment | "Also involved in the biosynthesis of cobalamin."xsd:string |
http://purl.uniprot.org/enzyme/2.1.1.107 | http://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/2.1.1.107 | http://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/2.1.1.107 | http://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/2.1.1.107 | http://www.w3.org/2004/02/skos/core#prefLabel | "uroporphyrinogen-III C-methyltransferase"xsd:string |
http://purl.uniprot.org/enzyme/2.1.1.107 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/2407234 |
http://purl.uniprot.org/enzyme/2.1.1.107 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/11980703 |
http://purl.uniprot.org/enzyme/2.1.1.107 | http://www.w3.org/2004/02/skos/core#altLabel | "uroporphyrin-III C-methyltransferase"xsd:string |
http://purl.uniprot.org/enzyme/2.1.1.107 | http://www.w3.org/2004/02/skos/core#altLabel | "SUMT"xsd:string |
http://purl.uniprot.org/enzyme/2.1.1.107 | http://www.w3.org/2004/02/skos/core#altLabel | "uroporphyrinogen III methylase"xsd:string |
http://purl.uniprot.org/enzyme/2.1.1.107 | http://www.w3.org/2004/02/skos/core#altLabel | "uroporphyrinogen-III methylase"xsd:string |
http://purl.uniprot.org/enzyme/2.1.1.107 | http://www.w3.org/2004/02/skos/core#altLabel | "uroporphyrinogen-III methyltransferase"xsd:string |
http://purl.uniprot.org/enzyme/2.1.1.107 | http://www.w3.org/2004/02/skos/core#altLabel | "S-adenosyl-L-methionine-dependent uroporphyrinogen III methylase"xsd:string |
http://purl.uniprot.org/enzyme/2.1.1.107 | http://www.w3.org/2004/02/skos/core#altLabel | "urogen III methylase"xsd:string |
http://purl.uniprot.org/enzyme/2.1.1.107 | http://www.w3.org/2004/02/skos/core#altLabel | "uroporphyrinogen methyltransferase"xsd:string |
http://purl.uniprot.org/enzyme/2.1.1.107 | http://www.w3.org/2004/02/skos/core#altLabel | "adenosylmethionine-uroporphyrinogen III methyltransferase"xsd:string |
http://purl.uniprot.org/enzyme/2.1.1.107 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/2.1.1.107#SIPB782F7060DAF84BE |
http://purl.uniprot.org/enzyme/2.1.1.107 | http://www.w3.org/2004/02/skos/core#broaderTransitive | http://purl.uniprot.org/enzyme/2.1.1.- |