(data stored in SCRATCH zone)

SWISSPROT: 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   08-MAY-2019, entry version 130.
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.,
RA   Mau B., 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
RT   MG1655 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
RT   succinate to 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
RT   methylmalonyl CoA decarboxylase from Escherichia coli.";
RL   Biochemistry 39:4630-4639(2000).
CC   -!- FUNCTION: Catalyzes the decarboxylation of (R)-methylmalonyl-CoA
CC       to propionyl-CoA. Could be part of a pathway that converts
CC       succinate to 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=Translation N-terminally shortened.; Evidence={ECO:0000305};
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_LN832404.1.
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   PDBsum; 1EF8; -.
DR   PDBsum; 1EF9; -.
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; 947408; -.
DR   KEGG; ecj:JW2886; -.
DR   KEGG; eco:b2919; -.
DR   PATRIC; fig|1411691.4.peg.3813; -.
DR   EchoBASE; EB2799; -.
DR   EcoGene; EG12972; scpB.
DR   eggNOG; ENOG4108M7F; Bacteria.
DR   eggNOG; COG1024; LUCA.
DR   HOGENOM; HOG000027939; -.
DR   InParanoid; P52045; -.
DR   KO; K11264; -.
DR   PhylomeDB; P52045; -.
DR   BioCyc; EcoCyc:G7516-MONOMER; -.
DR   BioCyc; ECOL316407:JW2886-MONOMER; -.
DR   BioCyc; MetaCyc:G7516-MONOMER; -.
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:0016853; F:isomerase 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;
DR   PRODOM; P52045.
DR   SWISS-2DPAGE; P52045.
KW   3D-structure; Complete proteome; Lyase; Reference proteome.
FT   CHAIN         1    261       Methylmalonyl-CoA decarboxylase.
FT                                /FTId=PRO_0000109355.
FT   REGION       64     68       Substrate binding.
FT   BINDING     110    110       Substrate; via amide nitrogen.
FT                                {ECO:0000269|PubMed:10769118}.
FT   BINDING     132    132       Substrate. {ECO:0000269|PubMed:10769118}.
FT   BINDING     253    253       Substrate. {ECO:0000269|PubMed:10769118}.
FT   STRAND        4     11       {ECO:0000244|PDB:1EF8}.
FT   STRAND       14     19       {ECO:0000244|PDB:1EF8}.
FT   HELIX        22     24       {ECO:0000244|PDB:1EF8}.
FT   HELIX        30     42       {ECO:0000244|PDB:1EF8}.
FT   STRAND       50     54       {ECO:0000244|PDB:1EF8}.
FT   STRAND       60     63       {ECO:0000244|PDB:1EF8}.
FT   HELIX        68     70       {ECO:0000244|PDB:1EF9}.
FT   STRAND       74     76       {ECO:0000244|PDB:1EF9}.
FT   STRAND       81     83       {ECO:0000244|PDB:1EF9}.
FT   HELIX        84     94       {ECO:0000244|PDB:1EF8}.
FT   STRAND       99    103       {ECO:0000244|PDB:1EF8}.
FT   STRAND      105    108       {ECO:0000244|PDB:1EF8}.
FT   HELIX       110    117       {ECO:0000244|PDB:1EF8}.
FT   STRAND      118    124       {ECO:0000244|PDB:1EF8}.
FT   STRAND      128    130       {ECO:0000244|PDB:1EF8}.
FT   HELIX       133    136       {ECO:0000244|PDB:1EF8}.
FT   HELIX       142    146       {ECO:0000244|PDB:1EF8}.
FT   STRAND      149    152       {ECO:0000244|PDB:1EF8}.
FT   HELIX       154    163       {ECO:0000244|PDB:1EF8}.
FT   HELIX       169    174       {ECO:0000244|PDB:1EF8}.
FT   STRAND      179    182       {ECO:0000244|PDB:1EF8}.
FT   HELIX       184    186       {ECO:0000244|PDB:1EF8}.
FT   HELIX       187    198       {ECO:0000244|PDB:1EF8}.
FT   HELIX       203    218       {ECO:0000244|PDB:1EF8}.
FT   HELIX       224    238       {ECO:0000244|PDB:1EF8}.
FT   HELIX       241    251       {ECO:0000244|PDB:1EF8}.
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
//

If you have problems or comments...

PBIL Back to PBIL home page