{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q1LJ80","uniProtkbId":"ATR_CUPMC","entryAudit":{"firstPublicDate":"2017-05-10","lastAnnotationUpdateDate":"2026-01-28","lastSequenceUpdateDate":"2006-05-30","entryVersion":101,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34)","commonName":"Ralstonia metallidurans","taxonId":266264,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Burkholderiales","Burkholderiaceae","Cupriavidus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"28130442"}],"value":"Cobalamin adenosyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"28130442"}],"value":"ATR"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28130442"}],"value":"2.5.1.-"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"ABF09796.1"}],"value":"cobO"},"orderedLocusNames":[{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"ABF09796.1"}],"value":"Rmet_2923"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28130442"}],"value":"Adenosyltransferase that catalyzes the conversion of cob(II)alamin to adenosylcob(III)alamin (AdoCbl) in the presence of ATP and an electron donor. Acts as an accessory protein of IcmF that functions in cofactor repair, since IcmF is prone to inactivation during catalytic turnover due to the occasional loss of the 5'-deoxyadenosine moiety and formation of the inactive cob(II)alamin cofactor in its active site. Thus, receives and repairs the inactive cofactor, which is then reloaded onto IcmF in a GTPase-gated step"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 cob(II)alamin + AH2 + 2 ATP = 2 adenosylcob(III)alamin + 2 triphosphate + A + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:53304"},{"database":"ChEBI","id":"CHEBI:13193"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16304"},{"database":"ChEBI","id":"CHEBI:17499"},{"database":"ChEBI","id":"CHEBI:18036"},{"database":"ChEBI","id":"CHEBI:18408"},{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28130442"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28130442"}],"value":"Is potentially allosterically regulated by GTP/GDP, which enhances its affinity for AdoCbl by 5-fold. Binds cob(II)alamin weakly in the absence of ATP. The presence of ATP (but not GTP or GDP) increases the affinity of cob(II)alamin for the enzyme, and stoichiometric binding is observed. GTP blocks the transfer of cob(II)alamin to IcmF from ATR, thus averting its reconstitution with inactive cofactor"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":2.3,"unit":"uM","substrate":"ATP","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28130442"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28130442"}],"value":"kcat is 3.8 min(-1)."}]}}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28130442"}],"value":"Homotrimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the Cob(I)alamin adenosyltransferase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":184,"modifier":"EXACT"}},"description":"Cobalamin adenosyltransferase","featureId":"PRO_0000439947"},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":21,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96EY8"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":18,"modifier":"EXACT"},"end":{"value":19,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96EY8"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96EY8"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":130,"modifier":"EXACT"},"end":{"value":134,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96EY8"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":154,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96EY8"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"id":"KW-0169","category":"Biological process","name":"Cobalamin biosynthesis"},{"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"20463976","citationType":"journal article","authors":["Janssen P.J.","Van Houdt R.","Moors H.","Monsieurs P.","Morin N.","Michaux A.","Benotmane M.A.","Leys N.","Vallaeys T.","Lapidus A.","Monchy S.","Medigue C.","Taghavi S.","McCorkle S.","Dunn J.","van der Lelie D.","Mergeay M."],"citationCrossReferences":[{"database":"PubMed","id":"20463976"},{"database":"DOI","id":"10.1371/journal.pone.0010433"}],"title":"The complete genome sequence of Cupriavidus metallidurans strain CH34, a master survivalist in harsh and anthropogenic environments.","publicationDate":"2010","journal":"PLoS ONE","firstPage":"E10433","lastPage":"E10433","volume":"5"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 43123 / DSM 2839 / NBRC 102507 / CH34","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"28130442","citationType":"journal article","authors":["Li Z.","Kitanishi K.","Twahir U.T.","Cracan V.","Chapman D.","Warncke K.","Banerjee R."],"citationCrossReferences":[{"database":"PubMed","id":"28130442"},{"database":"DOI","id":"10.1074/jbc.m117.775957"}],"title":"Cofactor editing by the G-protein metallochaperone domain regulates the radical B12 enzyme IcmF.","publicationDate":"2017","journal":"J. Biol. 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