ID   MUTA_STRCM              Reviewed;         616 AA.
AC   Q05064;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Methylmalonyl-CoA mutase small subunit;
DE            EC=5.4.99.2;
DE   AltName: Full=MCM-beta;
GN   Name=mutA;
OS   Streptomyces cinnamonensis.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces virginiae group.
OX   NCBI_TaxID=1900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A3823.5;
RX   PubMed=8099072; DOI=10.1128/jb.175.11.3511-3519.1993;
RA   Birch A., Leiser A., Robinson J.A.;
RT   "Cloning, sequencing, and expression of the gene encoding methylmalonyl-
RT   coenzyme A mutase from Streptomyces cinnamonensis.";
RL   J. Bacteriol. 175:3511-3519(1993).
CC   -!- FUNCTION: Catalyzes the isomerization of succinyl-CoA to methylmalonyl-
CC       CoA during synthesis of propionate from tricarboxylic acid-cycle
CC       intermediates. This conversion most likely represents an important
CC       source of building blocks for polyketide antibiotic biosynthesis. It is
CC       unable to catalyze the conversion of isobutyryl-CoA into N-butyryl-CoA.
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   -!- 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; L10064; AAA03040.1; -; Unassigned_DNA.
DR   PIR; A40595; A40595.
DR   AlphaFoldDB; Q05064; -.
DR   SMR; Q05064; -.
DR   UniPathway; UPA00945; UER00910.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
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   Gene3D; 1.10.196.20; -; 1.
DR   InterPro; IPR016176; Cbl-dep_enz_cat.
DR   InterPro; IPR024067; Me-malonyl-CoA_mutase_sm_su_N.
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   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..616
FT                   /note="Methylmalonyl-CoA mutase small subunit"
FT                   /id="PRO_0000194269"
SQ   SEQUENCE   616 AA;  65041 MW;  09CA24006E169AE6 CRC64;
     MTVLPDDGLS LAAEFPDATH EQWHRLVEGV VRKSGKDVSG TAAEEALSTT LEDGLTTRPL
     YTARDAAPDA GFPGFAPFVR GSVPEGNTPG GWDVRQRYAS ADPARTNEAV LTDLENGVTS
     LWLTLGSAGL PVTGLERALD GVYLDLVPVA LDAGSEAATA ARELLRLYEA AGVADDAVRG
     TLGADPLGHE ARTGEKSTSF AAVAELARLC GERYPGLRAL TVDALPYHEA GASAAQELGA
     SLATGVEYLR ALHDKGLGVE KAFAQLEFRF AATADQFLTI AKLRAARRLW ARVAEVSGVP
     AAGAQRQHAV TSPVMMTRRD PWVNMLRTTV ACLGAGVGGA DAVTVLPFDH ELGLPDAFAR
     RIARNTSTIL LEESHLARVI DPAGGSWYVE RLTDELAHAA WDFFKEIERA DGQVAALRSG
     LVGDRIAATW AERRKKLARR REPITGVSEF PLLTERPVER EPAPAAPPGG LPRVRRDEAY
     EELRGRSDAH LEATGARPKV FIAALGPAAA HTARATFAAN LFMAGGVEPV HDPVSVDAET
     AAEAFAASGA TVACLCSSDV LYAEQAEAVA RALKSAGALR VFLAGRGEFA DIDEYVFAGC
     DAVAVLTSTL DRMGVA