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P52045 (SCPB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methylmalonyl-CoA decarboxylase

Short name=MMCD
EC=4.1.1.41
Alternative name(s):
Transcarboxylase
Gene names
Name:scpB
Synonyms:mmcD, ygfG
Ordered Locus Names:b2919, JW2886
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length261 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the decarboxylation of methylmalonyl-CoA to propionyl-CoA. Could be part of a pathway that converts succinate to propionate. Ref.3

Catalytic activity

(S)-methylmalonyl-CoA = propanoyl-CoA + CO2. Ref.3

Subunit structure

Dimer of homotrimers. Ref.4

Sequence similarities

Belongs to the enoyl-CoA hydratase/isomerase family.

Sequence caution

The sequence AAA69086.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 261261Methylmalonyl-CoA decarboxylase
PRO_0000109355

Regions

Region64 – 685Substrate binding

Sites

Binding site1101Substrate; via amide nitrogen
Binding site1321Substrate
Binding site2531Substrate

Secondary structure

.................................................. 261
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P52045 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: B6A8A13EC2C2EBE0

FASTA26129,173
        10         20         30         40         50         60 
MSYQYVNVVT INKVAVIEFN YGRKLNALSK VFIDDLMQAL SDLNRPEIRC IILRAPSGSK 

        70         80         90        100        110        120 
VFSAGHDIHE LPSGGRDPLS YDDPLRQITR MIQKFPKPII SMVEGSVWGG AFEMIMSSDL 

       130        140        150        160        170        180 
IIAASTSTFS MTPVNLGVPY NLVGIHNLTR DAGFHIVKEL IFTASPITAQ RALAVGILNH 

       190        200        210        220        230        240 
VVEVEELEDF TLQMAHHISE KAPLAIAVIK EELRVLGEAH TMNSDEFERI QGMRRAVYDS 

       250        260 
EDYQEGMNAF LEKRKPNFVG H 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[2]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"Discovering new enzymes and metabolic pathways: conversion of succinate to propionate by Escherichia coli."
Haller T., Buckel T., Retey J., Gerlt J.A.
Biochemistry 39:4622-4629(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
Strain: K12 / MG1655 / ATCC 47076.
[4]"New reactions in the crotonase superfamily: structure of methylmalonyl CoA decarboxylase from Escherichia coli."
Benning M.M., Haller T., Gerlt J.A., Holden H.M.
Biochemistry 39:4630-4639(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U28377 Genomic DNA. Translation: AAA69086.1. Different initiation.
U00096 Genomic DNA. Translation: AAC75956.2.
AP009048 Genomic DNA. Translation: BAE76983.1.
RefSeqNP_417394.4. NC_000913.3.
YP_491119.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EF8X-ray1.85A/B/C1-261[»]
1EF9X-ray2.70A1-261[»]
ProteinModelPortalP52045.
SMRP52045. Positions 1-261.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING511145.b2919.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75956; AAC75956; b2919.
BAE76983; BAE76983; BAE76983.
GeneID12930444.
947408.
KEGGecj:Y75_p2850.
eco:b2919.
PATRIC32121252. VBIEscCol129921_3014.

Organism-specific databases

EchoBASEEB2799.
EcoGeneEG12972. scpB.

Phylogenomic databases

eggNOGCOG1024.
HOGENOMHOG000027939.
KOK11264.
OMAIEFNYAR.
OrthoDBEOG6M9F0M.
PhylomeDBP52045.
ProtClustDBPRK11423.

Enzyme and pathway databases

BioCycEcoCyc:G7516-MONOMER.
ECOL316407:JW2886-MONOMER.
MetaCyc:G7516-MONOMER.

Gene expression databases

GenevestigatorP52045.

Family and domain databases

Gene3D1.10.12.10. 1 hit.
InterProIPR014748. Crontonase_C.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view]
PfamPF00378. ECH. 1 hit.
[Graphical view]
PROSITEPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP52045.
PROP52045.

Entry information

Entry nameSCPB_ECOLI
AccessionPrimary (citable) accession number: P52045
Secondary accession number(s): P76643, Q2M9S3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene