CCCR_CERS4
ID CCCR_CERS4 Reviewed; 430 AA.
AC Q3IZ91; B8XVS5;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Crotonyl-CoA carboxylase/reductase {ECO:0000303|PubMed:17548827};
DE EC=1.3.1.85 {ECO:0000269|PubMed:17548827, ECO:0000269|PubMed:18819910, ECO:0000269|PubMed:19458256};
GN Name=ccr {ECO:0000303|PubMed:17548827}; OrderedLocusNames=RHOS4_25750;
GN ORFNames=RSP_0960;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, LACK OF METAL BINDING, AND
RP INDUCTION.
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RX PubMed=17548827; DOI=10.1073/pnas.0702791104;
RA Erb T.J., Berg I.A., Brecht V., Muller M., Fuchs G., Alber B.E.;
RT "Synthesis of C5-dicarboxylic acids from C2-units involving crotonyl-CoA
RT carboxylase/reductase: the ethylmalonyl-CoA pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10631-10636(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RX PubMed=18819910; DOI=10.1074/jbc.m805527200;
RA Erb T.J., Retey J., Fuchs G., Alber B.E.;
RT "Ethylmalonyl-CoA mutase from Rhodobacter sphaeroides defines a new
RT subclade of coenzyme B12-dependent acyl-CoA mutases.";
RL J. Biol. Chem. 283:32283-32293(2008).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND REACTION
RP MECHANISM.
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RX PubMed=19458256; DOI=10.1073/pnas.0903939106;
RA Erb T.J., Brecht V., Fuchs G., Mueller M., Alber B.E.;
RT "Carboxylation mechanism and stereochemistry of crotonyl-CoA
RT carboxylase/reductase, a carboxylating enoyl-thioester reductase.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8871-8876(2009).
RN [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RX PubMed=22056933; DOI=10.1128/jb.05959-11;
RA Schneider K., Asao M., Carter M.S., Alber B.E.;
RT "Rhodobacter sphaeroides uses a reductive route via propionyl coenzyme A to
RT assimilate 3-hydroxypropionate.";
RL J. Bacteriol. 194:225-232(2012).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reductive carboxylation of
CC crotonyl-CoA ((2E)-butenoyl-CoA) to (2S)-ethylmalonyl-CoA, in the
CC presence of CO2 (PubMed:17548827, PubMed:18819910, PubMed:19458256).
CC This is a key reaction in the ethylmalonyl-CoA pathway for acetyl-CoA
CC assimilation required for R.sphaeroides growth on acetate as sole
CC carbon source (PubMed:17548827, PubMed:22056933). Is also able to
CC accept acryloyl-CoA as an alternative substrate, yielding (2S)-
CC methylmalonyl-CoA (PubMed:18819910, PubMed:19458256). To a lesser
CC extent, when CO2 is absent, the enzyme also catalyzes the reduction of
CC crotonyl-CoA to butanoyl-CoA (PubMed:17548827, PubMed:19458256).
CC {ECO:0000269|PubMed:17548827, ECO:0000269|PubMed:18819910,
CC ECO:0000269|PubMed:19458256, ECO:0000269|PubMed:22056933}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-ethylmalonyl-CoA + NADP(+) = (2E)-butenoyl-CoA + CO2 +
CC NADPH; Xref=Rhea:RHEA:28082, ChEBI:CHEBI:16526, ChEBI:CHEBI:57332,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:60909; EC=1.3.1.85;
CC Evidence={ECO:0000269|PubMed:17548827, ECO:0000269|PubMed:18819910,
CC ECO:0000269|PubMed:19458256};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28084;
CC Evidence={ECO:0000305|PubMed:17548827};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-methylmalonyl-CoA + NADP(+) = acryloyl-CoA + CO2 + NADPH;
CC Xref=Rhea:RHEA:60252, ChEBI:CHEBI:16526, ChEBI:CHEBI:57327,
CC ChEBI:CHEBI:57367, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000269|PubMed:18819910, ECO:0000269|PubMed:19458256};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoyl-CoA + NADP(+) = (2E)-butenoyl-CoA + H(+) + NADPH;
CC Xref=Rhea:RHEA:27906, ChEBI:CHEBI:15378, ChEBI:CHEBI:57332,
CC ChEBI:CHEBI:57371, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000269|PubMed:17548827};
CC -!- COFACTOR:
CC Note=Despite some sequence similarity to zinc-containing alcohol
CC dehydrogenases, this enzyme does not bind any metals.
CC {ECO:0000269|PubMed:17548827};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.4 mM for (2E)-butenoyl-CoA (in the reductive carboxylation
CC assay) {ECO:0000269|PubMed:17548827, ECO:0000269|PubMed:19458256};
CC KM=0.7 mM for NADPH (in the reductive carboxylation assay)
CC {ECO:0000269|PubMed:17548827, ECO:0000269|PubMed:19458256};
CC KM=0.2 mM for CO2 {ECO:0000269|PubMed:17548827,
CC ECO:0000269|PubMed:19458256};
CC KM=0.2 mM for ethylmalonyl-CoA (in the oxidative decarboxylation
CC assay) {ECO:0000269|PubMed:17548827};
CC KM=0.5 mM for acryloyl-CoA (in the reductive carboxylation assay)
CC {ECO:0000269|PubMed:19458256};
CC KM=0.2 mM for (2E)-butenoyl-CoA (in the reduction assay to butanoyl-
CC CoA) {ECO:0000269|PubMed:19458256};
CC Vmax=130 umol/min/mg enzyme for the reductive carboxylation of (2E)-
CC butenoyl-CoA {ECO:0000269|PubMed:17548827};
CC Vmax=12 umol/min/mg enzyme for the oxidative decarboxylation of
CC ethylmalonyl-CoA {ECO:0000269|PubMed:17548827};
CC Vmax=10 umol/min/mg enzyme for the reduction of (2E)-butenoyl-CoA to
CC butanoyl-CoA {ECO:0000269|PubMed:17548827};
CC Note=kcat is 104 sec(-1) for the reductive carboxylation of (2E)-
CC butenoyl-CoA (PubMed:17548827). Acryloyl-CoA is accepted as an
CC alternative substrate analog by the enzyme with 40% relative activity
CC (compared with Vmax of crotonyl-CoA carboxylation) (PubMed:19458256).
CC {ECO:0000269|PubMed:17548827, ECO:0000269|PubMed:19458256};
CC pH dependence:
CC Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:19458256};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17548827}.
CC -!- INDUCTION: Down-regulated in cells grown photoheterotrophically with
CC succinate. {ECO:0000269|PubMed:17548827}.
CC -!- DISRUPTION PHENOTYPE: No effect during photoheterotrophic
CC (anaerobic/light) growth on succinate or 3-hydroxypropionate, no growth
CC on acetate under the same conditions. {ECO:0000269|PubMed:22056933}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Crotonyl-CoA carboxylase/reductase subfamily. {ECO:0000305}.
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DR EMBL; FJ445411; ACJ71669.1; -; Genomic_DNA.
DR EMBL; CP000143; ABA80143.1; -; Genomic_DNA.
DR RefSeq; WP_002721248.1; NZ_CP030271.1.
DR RefSeq; YP_354044.1; NC_007493.2.
DR AlphaFoldDB; Q3IZ91; -.
DR SMR; Q3IZ91; -.
DR STRING; 272943.RSP_0960; -.
DR PRIDE; Q3IZ91; -.
DR EnsemblBacteria; ABA80143; ABA80143; RSP_0960.
DR KEGG; rsp:RSP_0960; -.
DR PATRIC; fig|272943.9.peg.2932; -.
DR eggNOG; COG0604; Bacteria.
DR OMA; DFNCWGQ; -.
DR OrthoDB; 884088at2; -.
DR PhylomeDB; Q3IZ91; -.
DR BRENDA; 1.3.1.85; 5383.
DR Proteomes; UP000002703; Chromosome 1.
DR GO; GO:0043880; F:crotonyl-CoA reductase activity; IEA:InterPro.
DR CDD; cd08246; crotonyl_coA_red; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR010085; Crot_CoA_red.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01751; crot-CoA-red; 1.
PE 1: Evidence at protein level;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..430
FT /note="Crotonyl-CoA carboxylase/reductase"
FT /id="PRO_0000420613"
SQ SEQUENCE 430 AA; 47684 MW; CB4ED5EA2752660D CRC64;
MALDVQSDIV AYDAPKKDLY EIGEMPPLGH VPKEMYAWAI RRERHGEPDQ AMQIEVVETP
SIDSHEVLVL VMAAGVNYNG IWAGLGVPVS PFDGHKQPYH IAGSDASGIV WAVGDKVKRW
KVGDEVVIHC NQDDGDDEEC NGGDPMFSPT QRIWGYETPD GSFAQFTRVQ AQQLMKRPKH
LTWEEAACYT LTLATAYRML FGHKPHDLKP GQNVLVWGAS GGLGSYAIQL INTAGANAIG
VISEEDKRDF VMGLGAKGVI NRKDFKCWGQ LPKVNSPEYN EWLKEARKFG KAIWDITGKG
INVDMVFEHP GEATFPVSSL VVKKGGMVVI CAGTTGFNCT FDVRYMWMHQ KRLQGSHFAN
LKQASAANQL MIERRLDPCM SEVFPWAEIP AAHTKMYRNQ HKPGNMAVLV QAPRTGLRTF
ADVLEAGRKA
