Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Methylmalonyl-CoA decarboxylase

Gene

scpB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the decarboxylation of methylmalonyl-CoA to propionyl-CoA. Could be part of a pathway that converts succinate to propionate.1 Publication

Catalytic activityi

(S)-methylmalonyl-CoA = propanoyl-CoA + CO2.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei110 – 1101Substrate; via amide nitrogen1 Publication
Binding sitei132 – 1321Substrate1 Publication
Binding sitei253 – 2531Substrate1 Publication

GO - Molecular functioni

  1. carboxy-lyase activity Source: UniProtKB
  2. methylmalonyl-CoA decarboxylase activity Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Methylmalonyl-CoA decarboxylase (EC:4.1.1.41)
Short name:
MMCD
Alternative name(s):
Transcarboxylase
Gene namesi
Name:scpB
Synonyms:mmcD, ygfG
Ordered Locus Names:b2919, JW2886
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG12972. scpB.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 261261Methylmalonyl-CoA decarboxylasePRO_0000109355Add
BLAST

Expressioni

Gene expression databases

GenevestigatoriP52045.

Interactioni

Subunit structurei

Dimer of homotrimers.1 Publication

Protein-protein interaction databases

STRINGi511145.b2919.

Structurei

Secondary structure

1
261
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 118Combined sources
Beta strandi14 – 196Combined sources
Helixi22 – 243Combined sources
Helixi30 – 4213Combined sources
Beta strandi50 – 545Combined sources
Beta strandi60 – 634Combined sources
Helixi68 – 703Combined sources
Beta strandi74 – 763Combined sources
Beta strandi81 – 833Combined sources
Helixi84 – 9411Combined sources
Beta strandi99 – 1035Combined sources
Beta strandi105 – 1084Combined sources
Helixi110 – 1178Combined sources
Beta strandi118 – 1247Combined sources
Beta strandi128 – 1303Combined sources
Helixi133 – 1364Combined sources
Helixi142 – 1465Combined sources
Beta strandi149 – 1524Combined sources
Helixi154 – 16310Combined sources
Helixi169 – 1746Combined sources
Beta strandi179 – 1824Combined sources
Helixi184 – 1863Combined sources
Helixi187 – 19812Combined sources
Helixi203 – 21816Combined sources
Helixi224 – 23815Combined sources
Helixi241 – 25111Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EF8X-ray1.85A/B/C1-261[»]
1EF9X-ray2.70A1-261[»]
ProteinModelPortaliP52045.
SMRiP52045. Positions 1-261.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52045.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni64 – 685Substrate binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1024.
HOGENOMiHOG000027939.
InParanoidiP52045.
KOiK11264.
OMAiKPVISMV.
OrthoDBiEOG6M9F0M.
PhylomeDBiP52045.

Family and domain databases

Gene3Di1.10.12.10. 1 hit.
3.90.226.10. 1 hit.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR014748. Crontonase_C.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view]
PfamiPF00378. ECH. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 1 hit.
PROSITEiPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P52045-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSYQYVNVVT INKVAVIEFN YGRKLNALSK VFIDDLMQAL SDLNRPEIRC
60 70 80 90 100
IILRAPSGSK VFSAGHDIHE LPSGGRDPLS YDDPLRQITR MIQKFPKPII
110 120 130 140 150
SMVEGSVWGG AFEMIMSSDL IIAASTSTFS MTPVNLGVPY NLVGIHNLTR
160 170 180 190 200
DAGFHIVKEL IFTASPITAQ RALAVGILNH VVEVEELEDF TLQMAHHISE
210 220 230 240 250
KAPLAIAVIK EELRVLGEAH TMNSDEFERI QGMRRAVYDS EDYQEGMNAF
260
LEKRKPNFVG H
Length:261
Mass (Da):29,173
Last modified:October 1, 1996 - v1
Checksum:iB6A8A13EC2C2EBE0
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28377 Genomic DNA. Translation: AAA69086.1. Different initiation.
U00096 Genomic DNA. Translation: AAC75956.2.
AP009048 Genomic DNA. Translation: BAE76983.1.
RefSeqiNP_417394.4. NC_000913.3.
YP_491119.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75956; AAC75956; b2919.
BAE76983; BAE76983; BAE76983.
GeneIDi12930444.
947408.
KEGGiecj:Y75_p2850.
eco:b2919.
PATRICi32121252. VBIEscCol129921_3014.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28377 Genomic DNA. Translation: AAA69086.1. Different initiation.
U00096 Genomic DNA. Translation: AAC75956.2.
AP009048 Genomic DNA. Translation: BAE76983.1.
RefSeqiNP_417394.4. NC_000913.3.
YP_491119.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EF8X-ray1.85A/B/C1-261[»]
1EF9X-ray2.70A1-261[»]
ProteinModelPortaliP52045.
SMRiP52045. Positions 1-261.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi511145.b2919.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75956; AAC75956; b2919.
BAE76983; BAE76983; BAE76983.
GeneIDi12930444.
947408.
KEGGiecj:Y75_p2850.
eco:b2919.
PATRICi32121252. VBIEscCol129921_3014.

Organism-specific databases

EchoBASEiEB2799.
EcoGeneiEG12972. scpB.

Phylogenomic databases

eggNOGiCOG1024.
HOGENOMiHOG000027939.
InParanoidiP52045.
KOiK11264.
OMAiKPVISMV.
OrthoDBiEOG6M9F0M.
PhylomeDBiP52045.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP52045.
PROiP52045.

Gene expression databases

GenevestigatoriP52045.

Family and domain databases

Gene3Di1.10.12.10. 1 hit.
3.90.226.10. 1 hit.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR014748. Crontonase_C.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view]
PfamiPF00378. ECH. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 1 hit.
PROSITEiPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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.

Entry informationi

Entry nameiSCPB_ECOLI
AccessioniPrimary (citable) accession number: P52045
Secondary accession number(s): P76643, Q2M9S3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: January 7, 2015
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.