ID   MUTA_PORGI              Reviewed;         618 AA.
AC   Q59676;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2003, sequence version 2.
DT   25-MAY-2022, entry version 137.
DE   RecName: Full=Methylmalonyl-CoA mutase small subunit;
DE            EC=5.4.99.2;
DE   AltName: Full=MCM-beta;
GN   Name=mutA; Synonyms=mcmA; OrderedLocusNames=PG_1656;
OS   Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=242619;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 53978 / W50;
RX   PubMed=8566763; DOI=10.1016/0378-1119(95)00682-6;
RA   Jackson C.A., Kirzbaum L., Dashper S., Reynolds E.C.;
RT   "Cloning, expression and sequence analysis of the genes encoding the
RT   heterodimeric methylmalonyl-CoA mutase of Porphyromonas gingivalis W50.";
RL   Gene 167:127-132(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-308 / W83;
RX   PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA   Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA   Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA   Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA   Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA   Fraser C.M.;
RT   "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT   gingivalis strain W83.";
RL   J. Bacteriol. 185:5591-5601(2003).
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.
CC   -!- SIMILARITY: Belongs to the methylmalonyl-CoA mutase family.
CC       {ECO:0000305}.
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DR   EMBL; L30136; AAB51083.1; -; Genomic_DNA.
DR   EMBL; AE015924; AAQ66675.1; -; Genomic_DNA.
DR   PIR; JC4559; JC4559.
DR   RefSeq; WP_005875479.1; NC_002950.2.
DR   AlphaFoldDB; Q59676; -.
DR   SMR; Q59676; -.
DR   STRING; 242619.PG_1656; -.
DR   EnsemblBacteria; AAQ66675; AAQ66675; PG_1656.
DR   GeneID; 29255692; -.
DR   KEGG; pgi:PG_1656; -.
DR   eggNOG; COG1884; Bacteria.
DR   HOGENOM; CLU_009523_6_0_10; -.
DR   OMA; WYVERLT; -.
DR   OrthoDB; 720283at2; -.
DR   UniPathway; UPA00945; UER00910.
DR   Proteomes; UP000000588; 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; Reference proteome.
FT   CHAIN           1..618
FT                   /note="Methylmalonyl-CoA mutase small subunit"
FT                   /id="PRO_0000194267"
FT   CONFLICT        332
FT                   /note="A -> R (in Ref. 1; AAB51083)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        428..431
FT                   /note="HQSV -> PVG (in Ref. 1; AAB51083)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   618 AA;  68739 MW;  11577936BE579B7C CRC64;
     MAKEKEKLFS EFPPVSREAW IDKITADLKG VPFEKKLVWR TNEGFNVNPF YRREDIEDLK
     TTTSLPDEYP YVRSTRMHNE WLVRQDIVVG DNVAEANEKA LDLLNKGVDS LGFYLKKVHI
     NVDTLAALLK DIELTAVELN FNCCITRAAD LLSAFSAYVK KVGADPNKCH GSVSYDPFKK
     QLVRGVSNPD WVKMTLPVMD AARELPAFRV LNVNAVNLSD AGAFITQELG YALAWGAELL
     DKLTDAGYKP EEIASRIKFN FGIGSNYFME IAKFRAARWL WAQIVGSYGD QYKNETAKIH
     QHATTSMWNK TVFDAHVNLL RTQTETMSAA IAGVDSITVL PFDVTYQQSD DFSERIARNQ
     QLLLKEECHF DKVIDPSAGS YYIETLTNSI GEEAWKLFLS VEDAGGFTQA AETASIQKAV
     NASNIKRHQS VATRREIFLG TNQFPNFTEV AGDKITLAQG EHDCNCVKSI EPLNFSRGAS
     EFEALRLATE KSGKTPVVFM LTIGNLAMRL ARSQFSSNFF GCAGYKLIDN LGFKSVEEGV
     DAALAAKADI VVLCSSDDEY AEYAPAAFDY LAGRAEFVVA GAPACMADLE AKGIRNYVHV
     KSNVLETLRA FNDKFGIR