{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q3IZ91","secondaryAccessions":["B8XVS5"],"uniProtkbId":"CCCR_CERS4","entryAudit":{"firstPublicDate":"2013-01-09","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2005-11-08","entryVersion":109,"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":"17548827"}],"value":"Crotonyl-CoA carboxylase/reductase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17548827"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18819910"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19458256"}],"value":"1.3.1.85"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"17548827"}],"value":"ccr"},"orderedLocusNames":[{"value":"RHOS4_25750"}],"orfNames":[{"value":"RSP_0960"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17548827"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18819910"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19458256"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22056933"}],"value":"Catalyzes the NADPH-dependent reductive carboxylation of crotonyl-CoA ((2E)-butenoyl-CoA) to (2S)-ethylmalonyl-CoA, in the presence of CO2 (PubMed:17548827, PubMed:18819910, PubMed:19458256). This is a key reaction in the ethylmalonyl-CoA pathway for acetyl-CoA assimilation required for R.sphaeroides growth on acetate as sole carbon source (PubMed:17548827, PubMed:22056933). Is also able to accept acryloyl-CoA as an alternative substrate, yielding (2S)-methylmalonyl-CoA (PubMed:18819910, PubMed:19458256). To a lesser extent, when CO2 is absent, the enzyme also catalyzes the reduction of crotonyl-CoA to butanoyl-CoA (PubMed:17548827, PubMed:19458256)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2S)-ethylmalonyl-CoA + NADP(+) = (2E)-butenoyl-CoA + CO2 + NADPH","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:28082"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:57332"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:60909"}],"ecNumber":"1.3.1.85","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17548827"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18819910"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19458256"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:28084"},"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"17548827"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(S)-methylmalonyl-CoA + NADP(+) = acryloyl-CoA + CO2 + NADPH","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:60252"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:57327"},{"database":"ChEBI","id":"CHEBI:57367"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18819910"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19458256"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"butanoyl-CoA + NADP(+) = (2E)-butenoyl-CoA + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:27906"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57332"},{"database":"ChEBI","id":"CHEBI:57371"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17548827"}]}},{"commentType":"COFACTOR","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17548827"}],"value":"Despite some sequence similarity to zinc-containing alcohol dehydrogenases, this enzyme does not bind any metals."}]}},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"maximumVelocities":[{"velocity":130.0,"unit":"umol/min/mg","enzyme":"enzyme for the reductive carboxylation of (2E)-butenoyl-CoA","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17548827"}]},{"velocity":12.0,"unit":"umol/min/mg","enzyme":"enzyme for the oxidative decarboxylation of ethylmalonyl-CoA","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17548827"}]},{"velocity":10.0,"unit":"umol/min/mg","enzyme":"enzyme for the reduction of (2E)-butenoyl-CoA to butanoyl-CoA","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17548827"}]}],"michaelisConstants":[{"constant":0.4,"unit":"mM","substrate":"(2E)-butenoyl-CoA (in the reductive carboxylation assay)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17548827"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19458256"}]},{"constant":0.7,"unit":"mM","substrate":"NADPH (in the reductive carboxylation assay)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17548827"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19458256"}]},{"constant":0.2,"unit":"mM","substrate":"CO2","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17548827"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19458256"}]},{"constant":0.2,"unit":"mM","substrate":"ethylmalonyl-CoA (in the oxidative decarboxylation assay)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17548827"}]},{"constant":0.5,"unit":"mM","substrate":"acryloyl-CoA (in the reductive carboxylation assay)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19458256"}]},{"constant":0.2,"unit":"mM","substrate":"(2E)-butenoyl-CoA (in the reduction assay to butanoyl-CoA)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19458256"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17548827"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19458256"}],"value":"kcat is 104 sec(-1) for the reductive carboxylation of (2E)-butenoyl-CoA (PubMed:17548827). Acryloyl-CoA is accepted as an alternative substrate analog by the enzyme with 40% relative activity (compared with Vmax of crotonyl-CoA carboxylation) (PubMed:19458256)."}]}},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19458256"}],"value":"Optimum pH is 7.5-8.0."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17548827"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17548827"}],"value":"Down-regulated in cells grown photoheterotrophically with succinate"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22056933"}],"value":"No effect during photoheterotrophic (anaerobic/light) growth on succinate or 3-hydroxypropionate, no growth on acetate under the same conditions"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the zinc-containing alcohol dehydrogenase family. Crotonyl-CoA carboxylase/reductase subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":430,"modifier":"EXACT"}},"description":"Crotonyl-CoA carboxylase/reductase","featureId":"PRO_0000420613"}],"keywords":[{"id":"KW-0521","category":"Ligand","name":"NADP"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"17548827","citationType":"journal article","authors":["Erb T.J.","Berg I.A.","Brecht V.","Muller M.","Fuchs G.","Alber B.E."],"citationCrossReferences":[{"database":"PubMed","id":"17548827"},{"database":"DOI","id":"10.1073/pnas.0702791104"}],"title":"Synthesis of C5-dicarboxylic acids from C2-units involving crotonyl-CoA carboxylase/reductase: the ethylmalonyl-CoA pathway.","publicationDate":"2007","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"10631","lastPage":"10636","volume":"104"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","FUNCTION","CATALYTIC ACTIVITY","BIOPHYSICOCHEMICAL PROPERTIES","SUBUNIT","LACK OF METAL BINDING","INDUCTION"],"referenceComments":[{"value":"ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"CI-KSL06CN6861B","citationType":"submission","authors":["Copeland A.","Lucas S.","Lapidus A.","Barry K.","Detter J.C.","Glavina T.","Hammon N.","Israni S.","Pitluck S.","Richardson P.","Mackenzie C.","Choudhary M.","Larimer F.","Hauser L.J.","Land M.","Donohue T.J.","Kaplan S."],"title":"Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.","publicationDate":"SEP-2005","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.","type":"STRAIN"}]},{"referenceNumber":3,"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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