MCM_CERS4
ID MCM_CERS4 Reviewed; 709 AA.
AC Q3J4D7;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Methylmalonyl-CoA mutase {ECO:0000303|PubMed:16856937, ECO:0000303|PubMed:18819910};
DE Short=MCM;
DE EC=5.4.99.2 {ECO:0000269|PubMed:18819910};
GN Name=mcm {ECO:0000303|PubMed:16856937, ECO:0000303|PubMed:18819910};
GN Synonyms=mcmA {ECO:0000312|EMBL:ABA78347.1};
GN ORFNames=RSP_2192 {ECO:0000312|EMBL:ABA78347.1};
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 IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION, 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=16856937; DOI=10.1111/j.1365-2958.2006.05238.x;
RA Alber B.E., Spanheimer R., Ebenau-Jehle C., Fuchs G.;
RT "Study of an alternate glyoxylate cycle for acetate assimilation by
RT Rhodobacter sphaeroides.";
RL Mol. Microbiol. 61:297-309(2006).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
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: Radical enzyme that catalyzes the transformation of (2R)-
CC methylmalonyl-CoA to succinyl-CoA. Is involved in the ethylmalonyl-CoA
CC pathway for acetyl-CoA assimilation required for R.sphaeroides growth
CC on acetate as sole carbon source. {ECO:0000269|PubMed:18819910,
CC ECO:0000305|PubMed:16856937}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-methylmalonyl-CoA = succinyl-CoA; Xref=Rhea:RHEA:22888,
CC ChEBI:CHEBI:57292, ChEBI:CHEBI:57326; EC=5.4.99.2;
CC Evidence={ECO:0000269|PubMed:18819910};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22889;
CC Evidence={ECO:0000305|PubMed:18819910};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000269|PubMed:18819910};
CC -!- PATHWAY: Metabolic intermediate metabolism; propanoyl-CoA degradation;
CC succinyl-CoA from propanoyl-CoA: step 3/3.
CC {ECO:0000305|PubMed:18819910}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O86028}.
CC -!- INDUCTION: Strongly up-regulated during growth on acetate as sole
CC carbon source. {ECO:0000269|PubMed:16856937}.
CC -!- SIMILARITY: Belongs to the methylmalonyl-CoA mutase family.
CC {ECO:0000305}.
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DR EMBL; CP000143; ABA78347.1; -; Genomic_DNA.
DR RefSeq; WP_011337301.1; NZ_CP030271.1.
DR RefSeq; YP_352248.1; NC_007493.2.
DR AlphaFoldDB; Q3J4D7; -.
DR SMR; Q3J4D7; -.
DR STRING; 272943.RSP_2192; -.
DR EnsemblBacteria; ABA78347; ABA78347; RSP_2192.
DR KEGG; rsp:RSP_2192; -.
DR PATRIC; fig|272943.9.peg.1091; -.
DR eggNOG; COG1884; Bacteria.
DR eggNOG; COG2185; Bacteria.
DR OMA; IAQKEWV; -.
DR PhylomeDB; Q3J4D7; -.
DR BioCyc; MetaCyc:MON-13591; -.
DR UniPathway; UPA00945; UER00910.
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:UniProtKB-EC.
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.
DR PROSITE; PS00544; METMALONYL_COA_MUTASE; 1.
PE 1: Evidence at protein level;
KW Cobalamin; Cobalt; Isomerase; Metal-binding; Reference proteome.
FT CHAIN 1..709
FT /note="Methylmalonyl-CoA mutase"
FT /id="PRO_0000447589"
FT DOMAIN 579..709
FT /note="B12-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00666"
FT BINDING 73..77
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22033"
FT BINDING 183..185
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22033"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22033"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22033"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22033"
FT BINDING 271..273
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22033"
FT BINDING 592
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:P22033"
SQ SEQUENCE 709 AA; 77034 MW; E349B7C746D07C2F CRC64;
MTEDLDAWRK LAEKELKGKS PDSLTWNTLE GIPVKPLYTR ADLAGMEHLD GLPGVAPFTR
GVRATMYAGR PWTIRQYAGF STAEASNAFY RKALAAGQQG VSVAFDLATH RGYDSDHPRV
VGDVGKAGVA IDSIEDMKIL FNGIPLEKIS VSMTMNGAVI PILANFIVTG EEQGVPRAAL
SGTIQNDILK EFMVRNTYIY PPEPSMRIIA DIIEYTSKEM PKFNSISISG YHMQEAGANL
VQELAYTLAD GREYVRAALA RGMNVDDFAG RLSFFFAIGM NFFMEAAKLR AARLLWHRIM
SEFAPKKPGS LMLRTHCQTS GVSLQEQDPY NNVIRTAYEA MSAALGGTQS LHTNALDEAI
ALPTEFSARI ARNTQIILQE ETGVTRVVDP LAGSYYVESL TAELAEKAWA LIEEVEAMGG
MTKAVASGMP KLRIEESAAR RQAAIDRGED VIVGVNKYRL AKEDPIEILD IDNVAVRDAQ
IARLEKMRAT RDEAACQAAL DELTRRAAEG GNLLEAAVDA SRARASVGEI SMAMEKVFGR
HRAEVKTLSG VYGAAYEGDD GFAQIQRDVE SFAEEEGRRP RMLVVKMGQD GHDRGAKVIA
TAFADIGFDV DVGTLFQTPE EAAQDAIDND VHVVGISSLA AGHKTLAPKL IEALKEKGAG
EILVICGGVI PQQDYDFLQQ AGVKAIFGPG TNIPSAAKHI LDLIREARS
