{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q9ZFV4","uniProtkbId":"EUTT_SALTY","entryAudit":{"firstPublicDate":"2000-05-30","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1999-05-01","entryVersion":120,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","taxonId":99287,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Salmonella"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Corrinoid adenosyltransferase EutT"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16636051"}],"value":"2.5.1.154"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"16636051"}],"value":"ATP:co(I)rrinoid adenosyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"24336938"}],"value":"ACAT"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"15516577"}],"value":"Cob(II)alamin adenosyltransferase EutT"}},{"fullName":{"value":"Ethanolamine utilization cobalamin adenosyltransferase"}},{"fullName":{"value":"Ethanolamine utilization corrinoid adenosyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"15516577"}],"value":"EutT adenosyltransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10464203"}],"value":"eutT"},"orderedLocusNames":[{"value":"STM2467"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15516577"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16636051"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24336938"}],"value":"Converts cyanocobalamin (CN-B12) to adenosylcobalamin (AdoCbl), the inducer of the eut operon (PubMed:15516577, PubMed:16636051, PubMed:24336938). Is not active on cobinamide nor other intermediates in the adenosylcobalamin synthetic pathway. Allows full induction of the eut operon (PubMed:15516577). Can use ADP, CTP and dATP in place of ATP, and cobinamide in place of cobalamin, none are as efficiently used as ATP and cobalamin (PubMed:16636051)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29531136"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3045078"}],"value":"Expression of the eut operon allows this bacteria to use ethanolamine (EA) as a carbon, nitrogen and energy source. It relies on cobalamin (vitamin B12) both as a cofactor for the ethanolamine ammonia-lyase (EAL) activity and to induce the operon (PubMed:3045078). EA enhances bacterial survival in macrophages in a concentration-dependent manner, suggesting it is an important nutrient during infection (PubMed:29531136)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 cob(II)alamin + reduced [electron-transfer flavoprotein] + 2 ATP + 2 H2O = 2 adenosylcob(III)alamin + oxidized [electron-transfer flavoprotein] + 2 phosphate + 2 diphosphate + 3 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:66828"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16304"},{"database":"ChEBI","id":"CHEBI:18408"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"}],"ecNumber":"2.5.1.154","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16636051"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 cob(II)inamide + reduced [electron-transfer flavoprotein] + 2 ATP + 2 H2O = 2 adenosylcob(III)inamide + oxidized [electron-transfer flavoprotein] + 2 phosphate + 2 diphosphate + 3 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:66824"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:2480"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:141013"}],"ecNumber":"2.5.1.154","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16636051"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"a divalent metal cation","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16636051"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24336938"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28045498"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60240"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16636051"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24336938"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28045498"}],"value":"Binds 1 divalent metal cation ion per homodimer with both subunits providing Cys ligands; Fe(2+) gives most activity and is possibly the physiological cofactor, followed by Zn(2+) and Co(2+) (PubMed:24336938, PubMed:28045498). Activity stimulated by Mn(2+) (PubMed:16636051)."}]}},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":10.0,"unit":"uM","substrate":"ATP","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16636051"}]},{"constant":4.1,"unit":"uM","substrate":"cob(I)alamin","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16636051"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16636051"}],"value":"kcat is 0.03 sec(-1)."}]}},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16636051"}],"value":"Optimum pH is 7.0."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3045078"}],"value":"Amine and polyamine degradation; ethanolamine degradation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24336938"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Bacterial microcompartment","id":"SL-0544"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3045078"}],"value":"Part of the 17-gene eut operon transcribed from a single promoter, induced by ethanolamine and adenosylcobalamin (AdoCbl, vitamin B12)"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10464203"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15516577"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16585748"}],"value":"A quadruple eutP-eutQ-eutT-eutD deletion is not impaired for aerobic growth on ethanolamine (EA) supplemented with cobalamin (vitamin B12) (PubMed:10464203). Can grow on EA as sole carbon source when AdoB12 is supplied; double cobA-eutT mutants do not grow with CN-B12 as a nitrogen source (PubMed:15516577). A non-polar deletion mutant grows on EA from pH 5.5 to pH 8.0, but does not grow at pH 8.5, no change in acetaldehyde release on EA plus vitamin B12 (PubMed:16585748)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the Cob(I)alamin adenosyltransferase family. 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No binding of Co(2+).","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24336938"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28045498"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":75,"modifier":"EXACT"},"end":{"value":75,"modifier":"EXACT"}},"description":"No effect in vivo or in vitro. No binding of Co(2+).","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24336938"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28045498"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":79,"modifier":"EXACT"},"end":{"value":79,"modifier":"EXACT"}},"description":"Does not complement deletion, 20% activity in vitro. Reduces metal content of enzyme, complements a deletion.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16636051"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24336938"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28045498"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":80,"modifier":"EXACT"},"end":{"value":80,"modifier":"EXACT"}},"description":"Does not complement deletion, 0.6% activity in vitro. 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