{"metadata":{"accession":"PF01923","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR016030","hierarchy":null,"name":{"name":"Cobalamin adenosyltransferase","short":"Cob_adeno_trans"},"description":[{"text":"<p>Cobalamin adenosyltransferase This family contains the gene products of PduO and EutT which are both cobalamin adenosyltransferases. PduO is a protein with ATP:cob(I)alamin adenosyltransferase activity. The main role of this protein is the conversion of inactive cobalamins to AdoCbl for 1,2-propanediol degradation [[cite:PUB00013593]].The EutT enzyme appears to be an adenosyl transferase, converting CNB12 to AdoB12 [[cite:PUB00009955]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":[{"title":"Cob(I)yrinic_acid_a,c-diamide_adenosyltransferase","extract":"<p>In molecular biology, <b>cob(I)yrinic acid a,c-diamide adenosyltransferase</b> EC <span class=\"external text\">2.5.1.17</span> is an enzyme which catalyses the conversion of cobalamin into one of its coenzyme forms, adenosylcobalamin. Adenosylcobalamin is required as a cofactor for the activity of certain enzymes. AdoCbl contains an adenosyl moiety liganded to the cobalt ion of cobalamin via a covalent Co-C bond.</p>","thumbnail":null}],"literature":{"PUB00013593":{"PMID":11160088,"ISBN":null,"volume":"183","issue":"5","year":2001,"title":"Functional genomic, biochemical, and genetic characterization of the Salmonella pduO gene, an ATP:cob(I)alamin adenosyltransferase gene.","URL":null,"raw_pages":"1577-84","medline_journal":"J Bacteriol","ISO_journal":"J. Bacteriol.","authors":["Johnson CL","Pechonick E","Park SD","Havemann GD","Leal NA","Bobik TA."],"DOI_URL":"http://dx.doi.org/10.1128/JB.183.5.1577-1584.2001"},"PUB00009955":{"PMID":10464203,"ISBN":null,"volume":"181","issue":"17","year":1999,"title":"The 17-gene ethanolamine (eut) operon of Salmonella typhimurium encodes five homologues of carboxysome shell proteins.","URL":null,"raw_pages":"5317-29","medline_journal":"J Bacteriol","ISO_journal":"J. Bacteriol.","authors":["Kofoid E","Rappleye C","Stojiljkovic I","Roth J."],"DOI_URL":"http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=10464203"}},"set_info":{"accession":"CL0601","name":"Cob_adeno_trans"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":37,"interactions":0,"matches":15721,"pathways":0,"proteins":15667,"proteomes":13951,"sets":1,"structural_models":{"alphafold":10554},"structures":52,"taxa":21483},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":388,"alignment:full":8469},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"1wy1","name":"Crystal Structure of the PH0671 protein from Pyrococcus horikoshii OT3"}}}