ECM_METEA
ID ECM_METEA Reviewed; 688 AA.
AC Q49115; C5AP83;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Ethylmalonyl-CoA mutase {ECO:0000303|PubMed:25448820};
DE EC=5.4.99.63 {ECO:0000269|PubMed:25448820};
GN Name=ecm {ECO:0000303|PubMed:25448820};
GN Synonyms=meaA {ECO:0000303|PubMed:8868443};
GN OrderedLocusNames=MexAM1_META1p0180;
OS Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB
OS 9133 / AM1) (Methylobacterium extorquens).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=272630;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1;
RX PubMed=8868443; DOI=10.1099/13500872-142-3-675;
RA Smith L.M., Meijer W.G., Dijkhuizen L., Goodwin P.M.;
RT "A protein having similarity with methylmalonyl-CoA mutase is required for
RT the assimilation of methanol and ethanol by Methylobacterium extorquens
RT AM1.";
RL Microbiology 142:675-684(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1;
RX PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y.,
RA Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W.,
RA Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E.,
RA Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D.,
RA Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J.,
RA Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C.,
RA Lidstrom M.E.;
RT "Methylobacterium genome sequences: a reference blueprint to investigate
RT microbial metabolism of C1 compounds from natural and industrial sources.";
RL PLoS ONE 4:E5584-E5584(2009).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1;
RX PubMed=8704985; DOI=10.1099/13500872-142-6-1459;
RA Chistoserdova L.V., Lidstrom M.E.;
RT "Molecular characterization of a chromosomal region involved in the
RT oxidation of acetyl-CoA to glyoxylate in the isocitrate-lyase-negative
RT methylotroph Methylobacterium extorquens AM1.";
RL Microbiology 142:1459-1468(1996).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND INDUCTION.
RC STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1;
RX PubMed=25448820; DOI=10.1128/jb.02478-14;
RA Good N.M., Martinez-Gomez N.C., Beck D.A., Lidstrom M.E.;
RT "Ethylmalonyl coenzyme A mutase operates as a metabolic control point in
RT Methylobacterium extorquens AM1.";
RL J. Bacteriol. 197:727-735(2015).
CC -!- FUNCTION: Radical enzyme that catalyzes the transformation of (2R)-
CC ethylmalonyl-CoA to (2S)-methylsuccinyl-CoA (PubMed:25448820). Is
CC involved in the ethylmalonyl-CoA pathway for acetyl-CoA assimilation
CC required for M.extorquens growth on one- and two-carbon compounds such
CC as ethylamine, methanol or ethanol as sole carbon source
CC (PubMed:8868443, PubMed:8704985, PubMed:25448820). This enzyme acts as
CC a regulatory metabolic control point in this pathway, that allows
CC M.extorquens to efficiently restore metabolic balance when challenged
CC with a sudden change in the growth substrate (PubMed:25448820).
CC {ECO:0000269|PubMed:25448820, ECO:0000269|PubMed:8704985,
CC ECO:0000269|PubMed:8868443}.
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:25448820};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45577;
CC Evidence={ECO:0000305|PubMed:25448820};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000269|PubMed:25448820};
CC -!- INDUCTION: Up-regulated during growth on ethylamine.
CC {ECO:0000269|PubMed:25448820}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene lose the ability to grow
CC on C1 (methanol and methylamine) and C2 (ethanol and ethylamine)
CC compounds, and also on beta-hydroxybutyrate, but they grow normally on
CC pyruvate. Growth on C1 and C2 compounds is restored by addition of
CC glyoxylate or glycolate, indicating that these mutants are unable to
CC convert acetyl-CoA into glyoxylate. {ECO:0000269|PubMed:8704985}.
CC -!- SIMILARITY: Belongs to the methylmalonyl-CoA mutase family.
CC {ECO:0000305}.
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DR EMBL; U28335; AAC44087.1; -; Genomic_DNA.
DR EMBL; CP001510; ACS38142.1; -; Genomic_DNA.
DR RefSeq; WP_003597279.1; NC_012808.1.
DR AlphaFoldDB; Q49115; -.
DR SMR; Q49115; -.
DR STRING; 272630.MexAM1_META1p0180; -.
DR EnsemblBacteria; ACS38142; ACS38142; MexAM1_META1p0180.
DR KEGG; mea:Mex_1p0180; -.
DR eggNOG; COG1884; Bacteria.
DR eggNOG; COG2185; Bacteria.
DR HOGENOM; CLU_009523_4_0_5; -.
DR OMA; QWSLRMQ; -.
DR OrthoDB; 154460at2; -.
DR Proteomes; UP000009081; Chromosome.
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.
FT CHAIN 1..688
FT /note="Ethylmalonyl-CoA mutase"
FT /id="PRO_0000194276"
FT DOMAIN 530..659
FT /note="B12-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00666"
FT REGION 666..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 543
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 688 AA; 75066 MW; D84BD366933C0403 CRC64;
MSAQASVAEV KRDKPWIIRT YAGHSTAAES NKLYRGNLAK GQTGLSVAFD LPTQTGYDPD
HELARGEVGK VGVSIAHLGD MRALFDQIPL AQMNTSMTIN ATAPWLLSLY LAVAEEQGAP
LAALQGTTQN DIIKEYLSRG TYVFPPAPSL RLTKDVILFT TKNVPKWNPM NVCSYHLQEA
GATPVQELSY ALAIAIAVLD TVRDDPDFDE ASFSDVFSRI SFFVNAGMRF VTEICKMRAF
AELWDEIAQE RYGITDAKKR IFRYGVQVNS LGLTEQQPEN NVHRILIEML AVTLSKRARA
RAVQLPAWNE ALGLPRPWDQ QWSMRMQQIL AFETDLLEYD DIFDGSTVIE ARVEALKEQT
RAELTRIAEI GGAVTAVEAG ELKRALVESN ARRISAIEKG EQIVVGVNKW QQGEPSPLTA
GDGAIFTVSE TVEMEAETRI REWRSKRDER AVGQALADLE QAARSGANIM PPSIAAAKAG
VTTGEWGQRL REVFGEYRAP TGVTLQTVTS GAAEDARLLI ADLGERLGET PRLVVGKPGL
DGHSNGAEQI ALRARDVGFD VTYDGIRQTP TEIVAKAKER GAHVIGLSVL SGSHVPLVRE
VKAKLREAGL DHVPVVVGGI ISTEDELVLK NMGVTAVYTP KDYELDKIMV GLAKVVERAL
DKRAADRADT EAGVPGAPKR NESGAQVF
