ID   MUTA_MYCTO              Reviewed;         615 AA.
AC   P9WJK6; L0T9S6; P65485; P71773;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Probable methylmalonyl-CoA mutase small subunit;
DE            Short=MCM;
DE            EC=5.4.99.2;
GN   Name=mutA; OrderedLocusNames=MT1539;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Catalyzes the isomerization of succinyl-CoA to methylmalonyl-
CC       CoA during synthesis of propionate from tricarboxylic acid-cycle
CC       intermediates. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Metabolic intermediate metabolism; propanoyl-CoA degradation;
CC       succinyl-CoA from propanoyl-CoA: step 3/3.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the methylmalonyl-CoA mutase family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK45806.1; -; Genomic_DNA.
DR   PIR; G70711; G70711.
DR   RefSeq; WP_003407585.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WJK6; -.
DR   SMR; P9WJK6; -.
DR   PRIDE; P9WJK6; -.
DR   EnsemblBacteria; AAK45806; AAK45806; MT1539.
DR   GeneID; 45425472; -.
DR   KEGG; mtc:MT1539; -.
DR   PATRIC; fig|83331.31.peg.1656; -.
DR   HOGENOM; CLU_009523_6_0_11; -.
DR   UniPathway; UPA00945; UER00910.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004494; F:methylmalonyl-CoA mutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019652; P:lactate fermentation to propionate and acetate; IEA:InterPro.
DR   InterPro; IPR016176; Cbl-dep_enz_cat.
DR   InterPro; IPR036724; Cobalamin-bd_sf.
DR   InterPro; IPR006099; MeMalonylCoA_mutase_a/b_cat.
DR   InterPro; IPR004608; MMCoA_mutase_b.
DR   Pfam; PF01642; MM_CoA_mutase; 1.
DR   SUPFAM; SSF51703; SSF51703; 1.
DR   SUPFAM; SSF52242; SSF52242; 1.
DR   TIGRFAMs; TIGR00642; mmCoA_mut_beta; 1.
DR   PROSITE; PS00544; METMALONYL_COA_MUTASE; 1.
PE   3: Inferred from homology;
KW   Cobalamin; Cobalt; Isomerase.
FT   CHAIN           1..615
FT                   /note="Probable methylmalonyl-CoA mutase small subunit"
FT                   /id="PRO_0000427813"
SQ   SEQUENCE   615 AA;  64744 MW;  82D52807A14BDA75 CRC64;
     MSIDVPERAD LEQVRGRWRN AVAGVLSKSN RTDSAQLGDH PERLLDTQTA DGFAIRALYT
     AFDELPEPPL PGQWPFVRGG DPLRDVHSGW KVAEAFPANG ATADTNAAVL AALGEGVSAL
     LIRVGESGVA PDRLTALLSG VYLNLAPVIL DAGADYRPAC DVMLALVAQL DPGQRDTLSI
     DLGADPLTAS LRDRPAPPIE EVVAVASRAA GERGLRAITV DGPAFHNLGA TAATELAATV
     AAAVAYLRVL TESGLVVSDA LRQISFRLAA DDDQFMTLAK MRALRQLWAR VAEVVGDPGG
     GAAVVHAETS LPMMTQRDPW VNMLRCTLAA FGAGVGGADT VLVHPFDVAI PGGFPGTAAG
     FARRIARNTQ LLLLEESHVG RVLDPAGGSW FVEELTDRLA RRAWQRFQAI EARGGFVEAH
     DFLAGQIAEC AARRADDIAH RRLAITGVNE YPNLGEPALP PGDPTSPVRR YAAGFEALRD
     RSDHHLARTG ARPRVLLLPL GPLAEHNIRT TFATNLLASG GIEAIDPGTV DAGTVGNAVA
     DAGSPSVAVI CGTDARYRDE VADIVQAARA AGVSRVYLAG PEKALGDAAH RPDEFLTAKI
     NVVQALSNLL TRLGA