SCPA_ECOLI
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 03-AUG-2022, entry version 157.
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; Proteobacteria; 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; P27253; -.
DR PRIDE; P27253; -.
DR EnsemblBacteria; AAC75954; AAC75954; b2917.
DR EnsemblBacteria; BAE76981; BAE76981; BAE76981.
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; PWGGSAY; -.
DR PhylomeDB; P27253; -.
DR BioCyc; EcoCyc:METHYLMALONYL-COA-MUT-MON; -.
DR BioCyc; MetaCyc:METHYLMALONYL-COA-MUT-MON; -.
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 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 Pfam; PF02310; B12-binding; 1.
DR Pfam; PF01642; MM_CoA_mutase; 1.
DR SUPFAM; SSF51703; SSF51703; 1.
DR SUPFAM; SSF52242; SSF52242; 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 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