ECM_CERS4
ID ECM_CERS4 Reviewed; 652 AA.
AC Q3IZ90; B8XVS6;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Ethylmalonyl-CoA mutase {ECO:0000303|PubMed:18819910};
DE EC=5.4.99.63 {ECO:0000269|PubMed:18819910};
GN Name=ecm {ECO:0000303|PubMed:18819910, ECO:0000312|EMBL:ACJ71670.1};
GN Synonyms=meaA {ECO:0000312|EMBL:ABA80144.1};
GN ORFNames=RSP_0961 {ECO:0000312|EMBL:ABA80144.1};
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 [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, DISRUPTION PHENOTYPE,
RP AND SUBUNIT.
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 [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.
CC -!- FUNCTION: Radical enzyme that catalyzes the transformation of (2R)-
CC ethylmalonyl-CoA to (2S)-methylsuccinyl-CoA. Is involved in the
CC ethylmalonyl-CoA pathway for acetyl-CoA assimilation required for
CC R.sphaeroides growth on acetate as sole carbon source. Is highly
CC specific for its substrate, ethylmalonyl-CoA, and accepts
CC methylmalonyl-CoA only at 0.2% relative activity.
CC {ECO:0000269|PubMed:18819910}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-ethylmalonyl-CoA = (2S)-methylsuccinyl-CoA;
CC Xref=Rhea:RHEA:45576, ChEBI:CHEBI:84866, ChEBI:CHEBI:85316;
CC EC=5.4.99.63; Evidence={ECO:0000269|PubMed:18819910};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45577;
CC Evidence={ECO:0000269|PubMed:18819910};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000269|PubMed:18819910};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=60 uM for (2R)-ethylmalonyl-CoA {ECO:0000269|PubMed:18819910};
CC Vmax=7 umol/min/mg enzyme with (2R)-ethylmalonyl-CoA as substrate
CC {ECO:0000269|PubMed:18819910};
CC pH dependence:
CC Optimum pH is 6.5-8.0. {ECO:0000269|PubMed:18819910};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18819910}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are able to grow with
CC carbon substrates that do not require the operation of the (complete)
CC ethylmalonyl-CoA pathway (succinate, propionate/HCO3(-), or acetate
CC plus glyoxylate) but are unable to use acetate or acetoacetate as the
CC sole carbon source. They show undetectable ethylmalonyl-CoA mutase
CC activity when grown with acetate plus glyoxylate, while are still able
CC to convert methylmalonyl-CoA to succinyl-CoA.
CC {ECO:0000269|PubMed:18819910}.
CC -!- SIMILARITY: Belongs to the methylmalonyl-CoA mutase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FJ445412; ACJ71670.1; -; Genomic_DNA.
DR EMBL; CP000143; ABA80144.1; -; Genomic_DNA.
DR RefSeq; WP_011338628.1; NZ_CP030271.1.
DR RefSeq; YP_354045.1; NC_007493.2.
DR AlphaFoldDB; Q3IZ90; -.
DR SMR; Q3IZ90; -.
DR STRING; 272943.RSP_0961; -.
DR EnsemblBacteria; ABA80144; ABA80144; RSP_0961.
DR KEGG; rsp:RSP_0961; -.
DR PATRIC; fig|272943.9.peg.2933; -.
DR eggNOG; COG1884; Bacteria.
DR eggNOG; COG2185; Bacteria.
DR OMA; QWSLRMQ; -.
DR OrthoDB; 154460at2; -.
DR PhylomeDB; Q3IZ90; -.
DR BRENDA; 5.4.99.63; 5383.
DR Proteomes; UP000002703; Chromosome 1.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004494; F:methylmalonyl-CoA mutase activity; IEA:InterPro.
DR InterPro; IPR006159; Acid_CoA_mut_C.
DR InterPro; IPR016176; Cbl-dep_enz_cat.
DR InterPro; IPR006158; Cobalamin-bd.
DR InterPro; IPR036724; Cobalamin-bd_sf.
DR InterPro; IPR006099; MeMalonylCoA_mutase_a/b_cat.
DR InterPro; IPR006098; MMCoA_mutase_a_cat.
DR Pfam; PF02310; B12-binding; 1.
DR Pfam; PF01642; MM_CoA_mutase; 1.
DR SUPFAM; SSF51703; SSF51703; 1.
DR SUPFAM; SSF52242; SSF52242; 1.
DR TIGRFAMs; TIGR00640; acid_CoA_mut_C; 1.
DR TIGRFAMs; TIGR00641; acid_CoA_mut_N; 1.
DR PROSITE; PS51332; B12_BINDING; 1.
PE 1: Evidence at protein level;
KW Cobalamin; Cobalt; Isomerase; Metal-binding; Reference proteome.
FT CHAIN 1..652
FT /note="Ethylmalonyl-CoA mutase"
FT /id="PRO_0000447588"
FT DOMAIN 519..647
FT /note="B12-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00666"
FT BINDING 532
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /ligand_part="Co"
FT /ligand_part_id="ChEBI:CHEBI:27638"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P11653"
SQ SEQUENCE 652 AA; 71190 MW; 1687A2FBE1BF190A CRC64;
MTQKDSPWLF RTYAGHSTAK ASNALYRTNL AKGQTGLSVA FDLPTQTGYD SDDALARGEV
GKVGVPICHL GDMRMLFDQI PLEQMNTSMT INATAPWLLA LYIAVAEEQG ADISKLQGTV
QNDLMKEYLS RGTYICPPRP SLRMITDVAA YTRVHLPKWN PMNVCSYHLQ EAGATPEQEL
AFALATGIAV LDDLRTKVPA EHFPAMVGRI SFFVNAGIRF VTEMCKMRAF VDLWDEICRD
RYGIEEEKYR RFRYGVQVNS LGLTEQQPEN NVYRILIEML AVTLSKKARA RAVQLPAWNE
ALGLPRPWDQ QWSLRMQQIL AYESDLLEYE DLFDGNPAIE RKVEALKDGA REELAHIEAM
GGAIEAIDYM KARLVESNAE RIARVETGET VVVGVNRWTS GAPSPLTTGD GAIMVADPEA
ERDQIARLEA WRAGRDGAAV AAALAELRRA ATSGENVMPA SIAAAKAGAT TGEWAAELRR
AFGEFRGPTG VARAPSNRTE GLDPIREAVQ AVSARLGRPL KFVVGKPGLD GHSNGAEQIA
ARARDCGMDI TYDGIRLTPA EIVAKAADER AHVLGLSILS GSHMPLVTEV LAEMRRAGLD
VPLIVGGIIP EEDAAELRAS GVAAVYTPKD FELNRIMMDI VGLVDRTALA AE
