EPI_CERS4
ID EPI_CERS4 Reviewed; 134 AA.
AC Q3IZP4;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Ethylmalonyl-CoA/methylmalonyl-CoA epimerase {ECO:0000303|PubMed:18819910};
DE EC=5.1.99.- {ECO:0000269|PubMed:18819910};
DE EC=5.1.99.1 {ECO:0000269|PubMed:18819910};
GN Name=epi {ECO:0000303|PubMed:18819910};
GN ORFNames=RSP_0812 {ECO:0000312|EMBL:ABA79990.1};
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 [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 [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBSTRATE SPECIFICITY.
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).
CC -!- FUNCTION: Promiscuous isomerase that catalyzes epimerization of both
CC ethylmalonyl-CoA and methylmalonyl-CoA. Has thus a dual role in the
CC ethylmalonyl-CoA pathway for acetyl-CoA assimilation required for
CC R.sphaeroides growth on acetate as sole carbon source.
CC {ECO:0000269|PubMed:18819910}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-ethylmalonyl-CoA = (2S)-ethylmalonyl-CoA;
CC Xref=Rhea:RHEA:59728, ChEBI:CHEBI:60909, ChEBI:CHEBI:85316;
CC Evidence={ECO:0000269|PubMed:18819910};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:59730;
CC Evidence={ECO:0000305|PubMed:18819910};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-methylmalonyl-CoA = (S)-methylmalonyl-CoA;
CC Xref=Rhea:RHEA:20553, ChEBI:CHEBI:57326, ChEBI:CHEBI:57327;
CC EC=5.1.99.1; Evidence={ECO:0000269|PubMed:18819910};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20555;
CC Evidence={ECO:0000305|PubMed:18819910};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:18819910};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:18819910};
CC Note=Can use Co(2+) or Mn(2+) as cofactor, but Mg(2+) and Ni(2+) cannot
CC support enzymatic activity. {ECO:0000269|PubMed:18819910};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=40 uM for (2S)-ethylmalonyl-CoA {ECO:0000269|PubMed:18819910};
CC KM=80 uM for (2S)-methylmalonyl-CoA {ECO:0000269|PubMed:18819910};
CC Vmax=110 umol/min/mg enzyme with (2S)-ethylmalonyl-CoA as substrate
CC {ECO:0000269|PubMed:18819910};
CC Vmax=120 umol/min/mg enzyme with (2S)-methylmalonyl-CoA as substrate
CC {ECO:0000269|PubMed:18819910};
CC -!- SIMILARITY: Belongs to the methylmalonyl-CoA epimerase family.
CC {ECO:0000305}.
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DR EMBL; CP000143; ABA79990.1; -; Genomic_DNA.
DR RefSeq; WP_002720998.1; NZ_CP030271.1.
DR RefSeq; YP_353891.1; NC_007493.2.
DR AlphaFoldDB; Q3IZP4; -.
DR SMR; Q3IZP4; -.
DR STRING; 272943.RSP_0812; -.
DR EnsemblBacteria; ABA79990; ABA79990; RSP_0812.
DR GeneID; 67447565; -.
DR KEGG; rsp:RSP_0812; -.
DR PATRIC; fig|272943.9.peg.2771; -.
DR eggNOG; COG0346; Bacteria.
DR OMA; IHHICYE; -.
DR PhylomeDB; Q3IZP4; -.
DR BRENDA; 5.1.99.1; 5383.
DR Proteomes; UP000002703; Chromosome 1.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004493; F:methylmalonyl-CoA epimerase activity; IEA:UniProtKB-EC.
DR CDD; cd07249; MMCE; 1.
DR Gene3D; 3.10.180.10; -; 1.
DR InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR InterPro; IPR017515; MeMalonyl-CoA_epimerase.
DR InterPro; IPR037523; VOC.
DR SUPFAM; SSF54593; SSF54593; 1.
DR TIGRFAMs; TIGR03081; metmalonyl_epim; 1.
DR PROSITE; PS51819; VOC; 1.
PE 1: Evidence at protein level;
KW Cobalt; Isomerase; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..134
FT /note="Ethylmalonyl-CoA/methylmalonyl-CoA epimerase"
FT /id="PRO_0000447590"
FT DOMAIN 4..134
FT /note="VOC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT ACT_SITE 130
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT BINDING 7
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000250|UniProtKB:Q96PE7"
FT BINDING 79
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000250|UniProtKB:Q96PE7"
FT BINDING 130
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000250|UniProtKB:Q96PE7"
SQ SEQUENCE 134 AA; 14267 MW; 3E9E7155236847E7 CRC64;
MIGRLNHVAI AVPDLEAAAA QYRNTLGAEV GAPQDEPDHG VTVIFITLPN TKIELLHPLG
EGSPIAGFLE KNPAGGIHHI CYEVEDILAA RDRLKEAGAR VLGSGEPKIG AHGKPVLFLH
PKDFNGCLVE LEQV
