ID   MUTB_STRCM              Reviewed;         733 AA.
AC   Q05065;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   16-JUN-2009, entry version 57.
DE   RecName: Full=Methylmalonyl-CoA mutase large subunit;
DE            EC=5.4.99.2;
DE   AltName: Full=MCM-alpha;
GN   Name=mutB;
OS   Streptomyces cinnamonensis.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Streptomycineae; Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A3823.5;
RX   MEDLINE=93273720; PubMed=8099072;
RA   Birch A., Leiser A., Robinson J.A.;
RT   "Cloning, sequencing, and expression of the gene encoding
RT   methylmalonyl-coenzyme A mutase from Streptomyces cinnamonensis.";
RL   J. Bacteriol. 175:3511-3519(1993).
CC   -!- FUNCTION: Catalyzes the isomerization of succinyl-CoA to
CC       methylmalonyl-CoA during synthesis of propionate from
CC       tricarboxylic acid-cycle intermediates. This conversion most
CC       likely represents an important source of building blocks for
CC       polyketide antibiotic biosynthesis. It is unable to catalyze the
CC       conversion of isobutyryl-CoA into N-butyryl-CoA.
CC   -!- CATALYTIC ACTIVITY: (R)-methylmalonyl-CoA = succinyl-CoA.
CC   -!- COFACTOR: Adenosylcobalamin.
CC   -!- PATHWAY: Metabolic intermediate metabolism; propionyl-CoA
CC       degradation; succinyl-CoA from propionyl-CoA: step 3/3.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC   -!- SIMILARITY: Belongs to the methylmalonyl-CoA mutase family.
CC   -!- SIMILARITY: Contains 1 B12-binding domain.
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DR   EMBL; L10064; AAA03041.1; -; Unassigned_DNA.
DR   PIR; B40595; B40595.
DR   HSSP; P11653; 1REQ.
DR   BRENDA; 5.4.99.2; 1647.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   GO; GO:0050897; F:cobalt ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004494; F:methylmalonyl-CoA mutase activity; IEA:EC.
DR   GO; GO:0008152; P:metabolic process; IEA:InterPro.
DR   InterPro; IPR006159; Acid_CoA_mut_C.
DR   InterPro; IPR014348; Cbl-dep_enz_cat-sub.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR006099; MMCoA_mutase_a/b_cat.
DR   InterPro; IPR006098; MMCoA_mutase_a_cat.
DR   Gene3D; G3DSA:3.40.50.280; B12_bd; 1.
DR   Gene3D; G3DSA:3.20.20.240; Cobalamin-dep_enz_cat; 1.
DR   Pfam; PF02310; B12-binding; 1.
DR   Pfam; PF01642; MM_CoA_mutase; 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   3: Inferred from homology;
KW   Cobalamin; Cobalt; Isomerase; Metal-binding.
FT   CHAIN         1    733       Methylmalonyl-CoA mutase large subunit.
FT                                /FTId=PRO_0000194275.
FT   DOMAIN      600    732       B12-binding.
FT   REGION      571    610       Methylmalonyl-CoA-binding site (By
FT                                similarity).
FT   METAL       613    613       Cobalt (cobalamin axial ligand) (By
FT                                similarity).
SQ   SEQUENCE   733 AA;  79455 MW;  F02EEB54A154FA59 CRC64;
     MRIPEFDDIE LGAGGGPSGS AEQWRAAVKE SVGKSESDLL WETPEGIAVK PLYTGADVEG
     LDFLETYPGV APYLRGPYPT MYVNQPWTIR QYAGFSTAEE SNAFYRRNLA AGQKGLSVAF
     DLPTHRGYDS DHPRVTGDVG MAGVAIDSIY DMRQLFDGIP LDKMTVSMTM NGAVLPVLAL
     YIVAAEEQGV PPEKLAGTIQ NDILKEFMVR NTYIYPPKPS MRIISDIFAY TSQKMPRYNS
     ISISGYHIQE AGATADLELA YTLADGVEYL RAGQEAGLDV DAFAPRLSFF WAIGMNFFME
     VAKLRAARLL WAKLVKQFDP KNAKSLSLRT HSQTSGWSLT AQDVFNNVTR TCVEAMAATQ
     GHTQSLHTNA LDEALALPTD FSARIARNTQ LLIQQESGTT RTIDPWGGSA YVEKLTYDLA
     RRAWQHIEEV EAAGGMAQAI DAGIPKLRVE EAAARTQARI DSGRQPVIGV NKYRVDTDEQ
     IDVLKVDNSS VRAQQIEKLR RLREERDDAA CQDALRALTA AAERGPGQGL EGNLLALAVD
     AARAKATVGE ISDALESVYG RHAGQIRTIS GVYRTEAGQS PSVERTRALV DAFDEAEGRR
     PRILVAKMGQ DGHDRGQKVI ASAFADLGFD VDVGPLFQTP AEVARQAVEA DVHIVGVSSL
     AAGHLTLVPA LREELAAEGR DDIMIVVGGV IPPQDVEALH EAGATAVFPP GTVIPDAAHD
     LVKRLAADLG HEL
//