ID   SCPA_ECOLI              Reviewed;         714 AA.
AC   P27253; Q2M9S5;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2003, sequence version 2.
DT   24-JAN-2024, entry version 163.
DE   RecName: Full=Methylmalonyl-CoA mutase;
DE            Short=MCM;
DE            EC=5.4.99.2;
GN   Name=scpA; Synonyms=sbm, yliK; OrderedLocusNames=b2917, JW2884;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=1355087; DOI=10.1128/jb.174.17.5763-5764.1992;
RA   Roy I., Leadlay P.F.;
RT   "Physical map location of the new Escherichia coli gene sbm.";
RL   J. Bacteriol. 174:5763-5764(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=10769117; DOI=10.1021/bi992888d;
RA   Haller T., Buckel T., Retey J., Gerlt J.A.;
RT   "Discovering new enzymes and metabolic pathways: conversion of succinate to
RT   propionate by Escherichia coli.";
RL   Biochemistry 39:4622-4629(2000).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX   PubMed=11955068; DOI=10.1021/bi015593k;
RA   Dayem L.C., Carney J.R., Santi D.V., Pfeifer B.A., Khosla C., Kealey J.T.;
RT   "Metabolic engineering of a methylmalonyl-CoA mutase-epimerase pathway for
RT   complex polyketide biosynthesis in Escherichia coli.";
RL   Biochemistry 41:5193-5201(2002).
RN   [6]
RP   SUBUNIT, AND INTERACTION WITH ARGK.
RX   PubMed=18950999; DOI=10.1016/j.micres.2008.08.006;
RA   Froese D.S., Dobson C.M., White A.P., Wu X., Padovani D., Banerjee R.,
RA   Haller T., Gerlt J.A., Surette M.G., Gravel R.A.;
RT   "Sleeping beauty mutase (sbm) is expressed and interacts with ygfd in
RT   Escherichia coli.";
RL   Microbiol. Res. 164:1-8(2009).
CC   -!- FUNCTION: Catalyzes the interconversion of succinyl-CoA and
CC       methylmalonyl-CoA. Could be part of a pathway that converts succinate
CC       to propionate. {ECO:0000269|PubMed:10769117,
CC       ECO:0000269|PubMed:11955068}.
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:10769117, ECO:0000269|PubMed:11955068};
CC   -!- COFACTOR:
CC       Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC         Evidence={ECO:0000269|PubMed:10769117, ECO:0000269|PubMed:11955068};
CC   -!- SUBUNIT: Homodimer. Interacts with ArgK. {ECO:0000269|PubMed:18950999}.
CC   -!- SIMILARITY: Belongs to the methylmalonyl-CoA mutase family.
CC       {ECO:0000305}.
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DR   EMBL; X66836; CAA47311.1; -; Genomic_DNA.
DR   EMBL; U28377; AAA69084.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75954.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76981.1; -; Genomic_DNA.
DR   PIR; D65076; D65076.
DR   RefSeq; NP_417392.1; NC_000913.3.
DR   RefSeq; WP_000073223.1; NZ_SSZK01000003.1.
DR   RefSeq; WP_000073228.1; NZ_CP047127.1.
DR   AlphaFoldDB; P27253; -.
DR   SMR; P27253; -.
DR   BioGRID; 4262330; 27.
DR   IntAct; P27253; 6.
DR   STRING; 511145.b2917; -.
DR   SwissLipids; SLP:000001257; -.
DR   PaxDb; 511145-b2917; -.
DR   EnsemblBacteria; AAC75954; AAC75954; b2917.
DR   GeneID; 945576; -.
DR   KEGG; ecj:JW2884; -.
DR   KEGG; eco:b2917; -.
DR   PATRIC; fig|1411691.4.peg.3815; -.
DR   EchoBASE; EB1414; -.
DR   eggNOG; COG1884; Bacteria.
DR   eggNOG; COG2185; Bacteria.
DR   HOGENOM; CLU_009523_3_1_6; -.
DR   InParanoid; P27253; -.
DR   OMA; IQEETHI; -.
DR   OrthoDB; 9762378at2; -.
DR   PhylomeDB; P27253; -.
DR   BioCyc; EcoCyc:METHYLMALONYL-COA-MUT-MONOMER; -.
DR   BioCyc; MetaCyc:METHYLMALONYL-COA-MUT-MONOMER; -.
DR   PRO; PR:P27253; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0031419; F:cobalamin binding; IDA:EcoCyc.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004494; F:methylmalonyl-CoA mutase activity; IDA:EcoCyc.
DR   GO; GO:0019678; P:propionate metabolic process, methylmalonyl pathway; IBA:GO_Central.
DR   CDD; cd02071; MM_CoA_mut_B12_BD; 1.
DR   CDD; cd03679; MM_CoA_mutase_alpha_like; 1.
DR   Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR   Gene3D; 3.20.20.240; Methylmalonyl-CoA mutase; 1.
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   NCBIfam; TIGR00640; acid_CoA_mut_C; 1.
DR   NCBIfam; TIGR00641; acid_CoA_mut_N; 1.
DR   PANTHER; PTHR48101:SF4; METHYLMALONYL-COA MUTASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR48101; METHYLMALONYL-COA MUTASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF02310; B12-binding; 1.
DR   Pfam; PF01642; MM_CoA_mutase; 1.
DR   SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 1.
DR   SUPFAM; SSF51703; Cobalamin (vitamin B12)-dependent enzymes; 1.
DR   PROSITE; PS51332; B12_BINDING; 1.
DR   PROSITE; PS00544; METMALONYL_COA_MUTASE; 1.
PE   1: Evidence at protein level;
KW   Cobalamin; Cobalt; Isomerase; Metal-binding; Reference proteome.
FT   CHAIN           1..714
FT                   /note="Methylmalonyl-CoA mutase"
FT                   /id="PRO_0000194277"
FT   DOMAIN          584..714
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00666"
FT   BINDING         597
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"
FT   CONFLICT        356
FT                   /note="A -> V (in Ref. 1; CAA47311)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   714 AA;  77871 MW;  65222F5EB2F4633A CRC64;
     MSNVQEWQQL ANKELSRREK TVDSLVHQTA EGIAIKPLYT EADLDNLEVT GTLPGLPPYV
     RGPRATMYTA QPWTIRQYAG FSTAKESNAF YRRNLAAGQK GLSVAFDLAT HRGYDSDNPR
     VAGDVGKAGV AIDTVEDMKV LFDQIPLDKM SVSMTMNGAV LPVLAFYIVA AEEQGVTPDK
     LTGTIQNDIL KEYLCRNTYI YPPKPSMRII ADIIAWCSGN MPRFNTISIS GYHMGEAGAN
     CVQQVAFTLA DGIEYIKAAI SAGLKIDDFA PRLSFFFGIG MDLFMNVAML RAARYLWSEA
     VSGFGAQDPK SLALRTHCQT SGWSLTEQDP YNNVIRTTIE ALAATLGGTQ SLHTNAFDEA
     LGLPTDFSAR IARNTQIIIQ EESELCRTVD PLAGSYYIES LTDQIVKQAR AIIQQIDEAG
     GMAKAIEAGL PKRMIEEASA REQSLIDQGK RVIVGVNKYK LDHEDETDVL EIDNVMVRNE
     QIASLERIRA TRDDAAVTAA LNALTHAAQH NENLLAAAVN AARVRATLGE ISDALEVAFD
     RYLVPSQCVT GVIAQSYHQS EKSASEFDAI VAQTEQFLAD NGRRPRILIA KMGQDGHDRG
     AKVIASAYSD LGFDVDLSPM FSTPEEIARL AVENDVHVVG ASSLAAGHKT LIPELVEALK
     KWGREDICVV AGGVIPPQDY AFLQERGVAA IYGPGTPMLD SVRDVLNLIS QHHD
//