{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q3IZ90","secondaryAccessions":["B8XVS6"],"uniProtkbId":"ECM_CERS4","entryAudit":{"firstPublicDate":"2019-07-03","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2005-11-08","entryVersion":101,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.)","commonName":"Rhodobacter sphaeroides","taxonId":272943,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Rhodobacterales","Paracoccaceae","Cereibacter"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"18819910"}],"value":"Ethylmalonyl-CoA mutase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18819910"}],"value":"5.4.99.63"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"18819910"},{"evidenceCode":"ECO:0000312","source":"EMBL","id":"ACJ71670.1"}],"value":"ecm"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"ABA80144.1"}],"value":"meaA"}],"orderedLocusNames":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"RHOS4_25760"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"ABA80144.1"}],"value":"RSP_0961"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18819910"}],"value":"Radical enzyme that catalyzes the transformation of (2R)-ethylmalonyl-CoA to (2S)-methylsuccinyl-CoA. Is involved in the ethylmalonyl-CoA pathway for acetyl-CoA assimilation required for R.sphaeroides growth on acetate as sole carbon source. Is highly specific for its substrate, ethylmalonyl-CoA, and accepts methylmalonyl-CoA only at 0.2% relative activity"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2R)-ethylmalonyl-CoA = (2S)-methylsuccinyl-CoA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:45576"},{"database":"ChEBI","id":"CHEBI:84866"},{"database":"ChEBI","id":"CHEBI:85316"}],"ecNumber":"5.4.99.63","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18819910"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:45577"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18819910"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"adenosylcob(III)alamin","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18819910"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18408"}}]},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"maximumVelocities":[{"velocity":7.0,"unit":"umol/min/mg","enzyme":"enzyme with (2R)-ethylmalonyl-CoA as substrate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18819910"}]}],"michaelisConstants":[{"constant":60.0,"unit":"uM","substrate":"(2R)-ethylmalonyl-CoA","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18819910"}]}]},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18819910"}],"value":"Optimum pH is 6.5-8.0."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18819910"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18819910"}],"value":"Cells lacking this gene are able to grow with carbon substrates that do not require the operation of the (complete) ethylmalonyl-CoA pathway (succinate, propionate/HCO3(-), or acetate plus glyoxylate) but are unable to use acetate or acetoacetate as the sole carbon source. They show undetectable ethylmalonyl-CoA mutase activity when grown with acetate plus glyoxylate, while are still able to convert methylmalonyl-CoA to succinyl-CoA"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the methylmalonyl-CoA mutase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":652,"modifier":"EXACT"}},"description":"Ethylmalonyl-CoA mutase","featureId":"PRO_0000447588"},{"type":"Domain","location":{"start":{"value":519,"modifier":"EXACT"},"end":{"value":647,"modifier":"EXACT"}},"description":"B12-binding","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00666"}]},{"type":"Binding site","location":{"start":{"value":532,"modifier":"EXACT"},"end":{"value":532,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18408"},{"database":"ChEBI","id":"CHEBI:27638"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P11653"}],"ligand":{"name":"adenosylcob(III)alamin","id":"ChEBI:CHEBI:18408"},"ligandPart":{"name":"Co","id":"ChEBI:CHEBI:27638"}}],"keywords":[{"id":"KW-0846","category":"Ligand","name":"Cobalamin"},{"id":"KW-0170","category":"Ligand","name":"Cobalt"},{"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"18819910","citationType":"journal article","authors":["Erb T.J.","Retey J.","Fuchs G.","Alber B.E."],"citationCrossReferences":[{"database":"PubMed","id":"18819910"},{"database":"DOI","id":"10.1074/jbc.m805527200"}],"title":"Ethylmalonyl-CoA mutase from Rhodobacter sphaeroides defines a new subclade of coenzyme B12-dependent acyl-CoA mutases.","publicationDate":"2008","journal":"J. 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