MCM_RHIME
ID MCM_RHIME Reviewed; 712 AA.
AC O86028;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 24-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Methylmalonyl-CoA mutase {ECO:0000303|PubMed:12844209, ECO:0000303|PubMed:9889346};
DE Short=MCM {ECO:0000303|PubMed:12844209};
DE EC=5.4.99.2 {ECO:0000269|PubMed:12844209, ECO:0000305|PubMed:9889346};
GN Name=bhbA {ECO:0000303|PubMed:9889346}; OrderedLocusNames=RB1449;
GN ORFNames=SMb20757;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OG Plasmid pSymB (megaplasmid 2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=SU47 / 1021;
RX PubMed=9889346; DOI=10.1016/s0378-1119(98)00555-1;
RA Charles T.C., Aneja P.;
RT "Methylmalonyl-CoA mutase encoding gene of Sinorhizobium meliloti.";
RL Gene 226:121-127(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481431; DOI=10.1073/pnas.161294698;
RA Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J.,
RA Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A.;
RT "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing
RT endosymbiont Sinorhizobium meliloti.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
RN [4]
RP PROTEIN SEQUENCE OF 2-11, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=1021;
RX PubMed=12844209; DOI=10.1007/s00203-003-0570-3;
RA Miyamoto E., Watanabe F., Charles T.C., Yamaji R., Inui H., Nakano Y.;
RT "Purification and characterization of homodimeric methylmalonyl-CoA mutase
RT from Sinorhizobium meliloti.";
RL Arch. Microbiol. 180:151-154(2003).
CC -!- FUNCTION: Radical enzyme that catalyzes the transformation of
CC methylmalonyl-CoA to succinyl-CoA. Is required for growth on the
CC polyhydroxyalkanoate degradation pathway intermediates 3-
CC hydroxybutyrate and acetoacetate as sole carbon source.
CC {ECO:0000269|PubMed:12844209, ECO:0000269|PubMed:9889346}.
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:12844209, ECO:0000305|PubMed:9889346};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000269|PubMed:12844209};
CC -!- COFACTOR:
CC Name=a monovalent cation; Xref=ChEBI:CHEBI:60242;
CC Evidence={ECO:0000269|PubMed:12844209};
CC Note=Monovalent cations such as NH4(+), Rb(+), Cs(+), K(+), Li(+) or
CC Na(+) are required for enzyme activity. {ECO:0000269|PubMed:12844209};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.11 mM for (R,S)-methylmalonyl-CoA (in the presence of 3 mM
CC NH4(+)) {ECO:0000269|PubMed:12844209};
CC KM=0.13 mM for (R,S)-methylmalonyl-CoA (in the absence of 3 mM
CC NH4(+)) {ECO:0000269|PubMed:12844209};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:12844209};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:12844209};
CC -!- PATHWAY: Metabolic intermediate metabolism; propanoyl-CoA degradation;
CC succinyl-CoA from propanoyl-CoA: step 3/3. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12844209,
CC ECO:0000305|PubMed:9889346}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show no methylmalonyl-CoA
CC mutase activity, in contrast to wild-type.
CC {ECO:0000269|PubMed:9889346}.
CC -!- SIMILARITY: Belongs to the methylmalonyl-CoA mutase family.
CC {ECO:0000305}.
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DR EMBL; AF080073; AAD13665.1; -; Genomic_DNA.
DR EMBL; AL591985; CAC49849.1; -; Genomic_DNA.
DR PIR; A96023; A96023.
DR RefSeq; NP_437989.1; NC_003078.1.
DR RefSeq; WP_010976251.1; NC_003078.1.
DR AlphaFoldDB; O86028; -.
DR SMR; O86028; -.
DR STRING; 266834.SM_b20757; -.
DR PRIDE; O86028; -.
DR EnsemblBacteria; CAC49849; CAC49849; SM_b20757.
DR GeneID; 61601358; -.
DR KEGG; sme:SM_b20757; -.
DR PATRIC; fig|266834.11.peg.6375; -.
DR eggNOG; COG1884; Bacteria.
DR eggNOG; COG2185; Bacteria.
DR HOGENOM; CLU_009523_3_1_5; -.
DR OMA; IAQKEWV; -.
DR UniPathway; UPA00945; UER00910.
DR Proteomes; UP000001976; Plasmid pSymB.
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; Direct protein sequencing; Isomerase; Metal-binding;
KW Plasmid; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12844209"
FT CHAIN 2..712
FT /note="Methylmalonyl-CoA mutase"
FT /id="PRO_0000194274"
FT DOMAIN 580..712
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 593
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"
FT CONFLICT 47
FT /note="G -> R (in Ref. 1; AAD13665)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="G -> R (in Ref. 1; AAD13665)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="N -> K (in Ref. 1; AAD13665)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 712 AA; 77501 MW; 44FFD1D30294C5E9 CRC64;
MTEKTIKDWE ALAEKELRVS PEGLVWHTPE GIDVKPLYTS DDMSGIGHLN SLPGFEPFVR
GPRATMYAGR PWTVRQYAGF STAEASNAFY RRNLAAGQQG VSVAFDLATH RGYDSDHPRV
QGDVGKAGVA IDSVEDMKIL FDGIPLDRIS VSMTMNGAVI PILASFIVAG EEQGVSRDKL
SGTIQNDILK EFMVRNTYIY PPEPSMRIVA DIIEYTAKEM PKFNSISISG YHMQEAGATL
VQELAFTLAD GREYVRAALA KGLNVDDFAG RLSFFFAIGM NFFMEAAKLR AARLLWTRIM
QEFKPEKASS LMLRTHCQTS GVSLQEQDPY NNIVRTAFEA MSAVLGGTQS LHTNSFDEAM
ALPTDFSARI ARNTQLILQH ETGVTKVVDP LAGSYYVESL TNELAEKAWG LIEEVEALGG
MTKAVNAGLP KRLIEEAATR RQAAVDRAEE VIVGVNKYRL ENEQPIDILQ IDNAAVRTAQ
VKRIEETRRR RDSQKMKQAL DALADVARSG KGNLLAAAVE AARARATVGE ITDAMREAFG
DYTAIPEVVT DIYGKAYEGD PELGVLAGRL GEATKRLGHK PKIMVAKLGQ DGHDRGAKVI
ASAFGDIGFD VVAGPLFQTP EEAADLALAE EVTVIGVSSL AAGHRTLMPQ LAEALKKRGG
EDIIVVCGGV IPRQDYDYLM ENGVAAVFGP GTQVLDAARA VLDLIEGKRR NV
