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http://purl.uniprot.org/enzyme/2.8.4.4http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/2.8.4.4http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/2.8.4.-
http://purl.uniprot.org/enzyme/2.8.4.4http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/2.-.-.-
http://purl.uniprot.org/enzyme/2.8.4.4http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/2.8.-.-
http://purl.uniprot.org/enzyme/2.8.4.4http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/2.8.4.4http://www.w3.org/2000/01/rdf-schema#comment"In the second reaction the enzyme catalyzes the reductive fragmentation of a second molecule of AdoMet, yielding a 5'-deoxyadenosine radical, which then attacks the methylated sulfur atom of the polysulfide bridge, resulting in the transfer of a methylsulfanyl group to aspartate(89) (Escherichia coli numbering)."xsd:string
http://purl.uniprot.org/enzyme/2.8.4.4http://www.w3.org/2000/01/rdf-schema#comment"The enzyme is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes."xsd:string
http://purl.uniprot.org/enzyme/2.8.4.4http://www.w3.org/2000/01/rdf-schema#comment"This bacterial enzyme binds two [4Fe-4S] clusters."xsd:string
http://purl.uniprot.org/enzyme/2.8.4.4http://www.w3.org/2000/01/rdf-schema#comment"In the first reaction the enzyme transfers a methyl group from AdoMet to the external sulfur ion of the sulfur bridge."xsd:string
http://purl.uniprot.org/enzyme/2.8.4.4http://www.w3.org/2000/01/rdf-schema#comment"A bridge of five sulfur atoms is formed between the free Fe atoms of the two [4Fe-4S] clusters."xsd:string
http://purl.uniprot.org/enzyme/2.8.4.4http://www.w3.org/2004/02/skos/core#prefLabel"[ribosomal protein uS12] (aspartate(89)-C(3))-methylthiotransferase"xsd:string
http://purl.uniprot.org/enzyme/2.8.4.4http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/20007320
http://purl.uniprot.org/enzyme/2.8.4.4http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/23542644
http://purl.uniprot.org/enzyme/2.8.4.4http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/23991893
http://purl.uniprot.org/enzyme/2.8.4.4http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/18252828
http://purl.uniprot.org/enzyme/2.8.4.4http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/19736993
http://purl.uniprot.org/enzyme/2.8.4.4http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/21169565
http://purl.uniprot.org/enzyme/2.8.4.4http://www.w3.org/2004/02/skos/core#altLabel"[ribosomal protein S12] (aspartate-C(3))-methylthiotransferase"xsd:string
http://purl.uniprot.org/enzyme/2.8.4.4http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/2.8.4.4#SIP23E17836B0944CD1
http://purl.uniprot.org/enzyme/2.8.4.4http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/2.8.4.4#SIPB4D2DA3C297B5745
http://purl.uniprot.org/enzyme/2.8.4.4http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/2.8.4.4#SIPF7EF0C328347A089
http://purl.uniprot.org/enzyme/2.8.4.4http://www.w3.org/2004/02/skos/core#broaderTransitivehttp://purl.uniprot.org/enzyme/2.8.4.-
http://purl.uniprot.org/uniprot/A0A9D9YIT3http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/2.8.4.4
http://purl.uniprot.org/uniprot/A0A0C1NES7http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/2.8.4.4
http://purl.uniprot.org/uniprot/A0A8J3WRZ3http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/2.8.4.4