| http://purl.uniprot.org/enzyme/2.5.1.17 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
| http://purl.uniprot.org/enzyme/2.5.1.17 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/2.5.1.- |
| http://purl.uniprot.org/enzyme/2.5.1.17 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/2.5.-.- |
| http://purl.uniprot.org/enzyme/2.5.1.17 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/2.-.-.- |
| http://purl.uniprot.org/enzyme/2.5.1.17 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
| http://purl.uniprot.org/enzyme/2.5.1.17 | http://www.w3.org/2000/01/rdf-schema#comment | "The enzyme can act on other corrinoids, such as cob(II)inamide."xsd:string |
| http://purl.uniprot.org/enzyme/2.5.1.17 | http://www.w3.org/2000/01/rdf-schema#comment | "The corrinoid adenosylation pathway comprises three steps: (i) reduction of Co(III) to Co(II) by a one-electron transfer."xsd:string |
| http://purl.uniprot.org/enzyme/2.5.1.17 | http://www.w3.org/2000/01/rdf-schema#comment | "In the anaerobic bacterium Salmonella enterica they are encoded by the cobA gene (a housekeeping enzyme involved in both adenosylcobalamin de novo biosynthesis and salvage), the pduO gene (involved in (S)-propane-1,2-diol utilization), and the eutT gene (involved in ethanolamine utilization)."xsd:string |
| http://purl.uniprot.org/enzyme/2.5.1.17 | http://www.w3.org/2000/01/rdf-schema#comment | "Three types of corrinoid adenosyltransferases, not related by sequence, have been described."xsd:string |
| http://purl.uniprot.org/enzyme/2.5.1.17 | http://www.w3.org/2000/01/rdf-schema#comment | "Since EutT hydrolyzes triphosphate during catalysis, it is classified as a separate enzyme."xsd:string |
| http://purl.uniprot.org/enzyme/2.5.1.17 | http://www.w3.org/2000/01/rdf-schema#comment | "(iii) the Co(I) conducts a nucleophilic attack on the adenosyl moiety of ATP, resulting in transfer of the deoxyadenosyl group and oxidation of the cobalt atom to Co(III) state."xsd:string |
| http://purl.uniprot.org/enzyme/2.5.1.17 | http://www.w3.org/2000/01/rdf-schema#comment | "The mammalian enzyme belongs to the PduO type."xsd:string |
| http://purl.uniprot.org/enzyme/2.5.1.17 | http://www.w3.org/2000/01/rdf-schema#comment | "This is followed by a second single-electron transfer from either free dihydroflavins or the reduced flavin cofactor of flavoproteins, resulting in reduction to Co(I)."xsd:string |
| http://purl.uniprot.org/enzyme/2.5.1.17 | http://www.w3.org/2000/01/rdf-schema#comment | "(ii) Co(II) is bound by corrinoid adenosyltransferase, resulting in displacement of the lower axial ligand by an aromatic residue."xsd:string |
| http://purl.uniprot.org/enzyme/2.5.1.17 | http://www.w3.org/2000/01/rdf-schema#comment | "The reduction potential of the 4-coordinate Co(II) intermediate is raised by ~250 mV compared with the free compound, bringing it to within physiological range."xsd:string |
| http://purl.uniprot.org/enzyme/2.5.1.17 | http://www.w3.org/2000/01/rdf-schema#comment | "This can occur non-enzymically in the presence of dihydroflavin nucleotides or reduced flavoproteins."xsd:string |
| http://purl.uniprot.org/enzyme/2.5.1.17 | http://www.w3.org/2004/02/skos/core#prefLabel | "corrinoid adenosyltransferase"xsd:string |
| http://purl.uniprot.org/enzyme/2.5.1.17 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/11148030 |
| http://purl.uniprot.org/enzyme/2.5.1.17 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/7860601 |
| http://purl.uniprot.org/enzyme/2.5.1.17 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/10894741 |
| http://purl.uniprot.org/enzyme/2.5.1.17 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/11408479 |
| http://purl.uniprot.org/enzyme/2.5.1.17 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/19933577 |
| http://purl.uniprot.org/enzyme/2.5.1.17 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/19236001 |
| http://purl.uniprot.org/enzyme/2.5.1.17 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/5946606 |
| http://purl.uniprot.org/enzyme/2.5.1.17 | http://www.w3.org/2004/02/skos/core#altLabel | "cob(I)yrinic acid a,c-diamide adenosyltransferase"xsd:string |