SCPB_ECOLI
ID SCPB_ECOLI Reviewed; 261 AA.
AC P52045; P76643; Q2M9S3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Methylmalonyl-CoA decarboxylase;
DE Short=MMCD;
DE EC=4.1.1.-;
DE AltName: Full=Transcarboxylase;
GN Name=scpB; Synonyms=mmcD, ygfG; OrderedLocusNames=b2919, JW2886;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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 [4]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, AND
RP SUBUNIT.
RX PubMed=10769118; DOI=10.1021/bi9928896;
RA Benning M.M., Haller T., Gerlt J.A., Holden H.M.;
RT "New reactions in the crotonase superfamily: structure of methylmalonyl CoA
RT decarboxylase from Escherichia coli.";
RL Biochemistry 39:4630-4639(2000).
CC -!- FUNCTION: Catalyzes the decarboxylation of (R)-methylmalonyl-CoA to
CC propionyl-CoA. Could be part of a pathway that converts succinate to
CC propanoate. {ECO:0000269|PubMed:10769117}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-methylmalonyl-CoA + H(+) = CO2 + propanoyl-CoA;
CC Xref=Rhea:RHEA:27666, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57326, ChEBI:CHEBI:57392;
CC Evidence={ECO:0000269|PubMed:10769117};
CC -!- SUBUNIT: Dimer of homotrimers. {ECO:0000269|PubMed:10769118}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA69086.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U28377; AAA69086.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC75956.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE76983.1; -; Genomic_DNA.
DR RefSeq; NP_417394.4; NC_000913.3.
DR RefSeq; WP_000122080.1; NZ_STEB01000001.1.
DR PDB; 1EF8; X-ray; 1.85 A; A/B/C=1-261.
DR PDB; 1EF9; X-ray; 2.70 A; A=1-261.
DR PDB; 6N92; X-ray; 1.70 A; A/B/C/D/E/F=1-261.
DR PDB; 6N93; X-ray; 1.70 A; A/B/C/D/E/F=1-261.
DR PDB; 6N94; X-ray; 1.75 A; A/B/C/D/E/F=1-261.
DR PDB; 6N95; X-ray; 1.80 A; A/B/C/D/E/F=1-261.
DR PDB; 6N96; X-ray; 1.70 A; A/B/C/D/E/F=1-261.
DR PDB; 6N97; X-ray; 1.75 A; A/B/C/D/E/F=1-261.
DR PDBsum; 1EF8; -.
DR PDBsum; 1EF9; -.
DR PDBsum; 6N92; -.
DR PDBsum; 6N93; -.
DR PDBsum; 6N94; -.
DR PDBsum; 6N95; -.
DR PDBsum; 6N96; -.
DR PDBsum; 6N97; -.
DR AlphaFoldDB; P52045; -.
DR SMR; P52045; -.
DR BioGRID; 4259438; 2.
DR STRING; 511145.b2919; -.
DR DrugBank; DB03117; 2-carboxypropyl-coenzyme A.
DR PaxDb; P52045; -.
DR PRIDE; P52045; -.
DR EnsemblBacteria; AAC75956; AAC75956; b2919.
DR EnsemblBacteria; BAE76983; BAE76983; BAE76983.
DR GeneID; 66673204; -.
DR GeneID; 947408; -.
DR KEGG; ecj:JW2886; -.
DR KEGG; eco:b2919; -.
DR PATRIC; fig|1411691.4.peg.3813; -.
DR EchoBASE; EB2799; -.
DR eggNOG; COG1024; Bacteria.
DR HOGENOM; CLU_009834_7_3_6; -.
DR InParanoid; P52045; -.
DR OMA; WRSVAFS; -.
DR PhylomeDB; P52045; -.
DR BioCyc; EcoCyc:G7516-MON; -.
DR BioCyc; MetaCyc:G7516-MON; -.
DR EvolutionaryTrace; P52045; -.
DR PRO; PR:P52045; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0016831; F:carboxy-lyase activity; ISS:UniProtKB.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IBA:GO_Central.
DR GO; GO:0004492; F:methylmalonyl-CoA decarboxylase activity; IDA:EcoCyc.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR Gene3D; 1.10.12.10; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR014748; Enoyl-CoA_hydra_C.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF52096; SSF52096; 1.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase; Reference proteome.
FT CHAIN 1..261
FT /note="Methylmalonyl-CoA decarboxylase"
FT /id="PRO_0000109355"
FT BINDING 64..68
FT /ligand="substrate"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10769118"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10769118"
FT BINDING 253
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10769118"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:6N92"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:6N92"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:6N92"
FT HELIX 30..42
FT /evidence="ECO:0007829|PDB:6N92"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:6N92"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:6N92"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:6N92"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:6N92"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:1EF9"
FT HELIX 84..94
FT /evidence="ECO:0007829|PDB:6N92"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:6N92"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:6N92"
FT HELIX 110..117
FT /evidence="ECO:0007829|PDB:6N92"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:6N92"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:6N92"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:6N92"
FT HELIX 142..146
FT /evidence="ECO:0007829|PDB:6N92"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:6N92"
FT HELIX 154..163
FT /evidence="ECO:0007829|PDB:6N92"
FT HELIX 169..174
FT /evidence="ECO:0007829|PDB:6N92"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:6N92"
FT HELIX 184..199
FT /evidence="ECO:0007829|PDB:6N92"
FT HELIX 203..218
FT /evidence="ECO:0007829|PDB:6N92"
FT HELIX 224..238
FT /evidence="ECO:0007829|PDB:6N92"
FT HELIX 241..251
FT /evidence="ECO:0007829|PDB:6N92"
SQ SEQUENCE 261 AA; 29173 MW; B6A8A13EC2C2EBE0 CRC64;
MSYQYVNVVT INKVAVIEFN YGRKLNALSK VFIDDLMQAL SDLNRPEIRC IILRAPSGSK
VFSAGHDIHE LPSGGRDPLS YDDPLRQITR MIQKFPKPII SMVEGSVWGG AFEMIMSSDL
IIAASTSTFS MTPVNLGVPY NLVGIHNLTR DAGFHIVKEL IFTASPITAQ RALAVGILNH
VVEVEELEDF TLQMAHHISE KAPLAIAVIK EELRVLGEAH TMNSDEFERI QGMRRAVYDS
EDYQEGMNAF LEKRKPNFVG H
