P52045 (SCPB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	261 AA.
Sequence status	Complete.
Protein existence	Evidence 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

Keywords
Molecular function	Lyase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	cytosol Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	methylmalonyl-CoA decarboxylase activity Inferred from direct assay Ref.3. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 261

261

Methylmalonyl-CoA decarboxylase

PRO_0000109355

Regions

Region

64 – 68

5

Substrate binding

Sites

Binding site

110

1

Substrate; via amide nitrogen

Binding site

132

1

Substrate

Binding site

253

1

Substrate

Secondary structure

1

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261

Helix Strand Turn

Details...

Beta strand

4 – 11

8

Beta strand

14 – 19

6

Helix

22 – 24

3

Helix

30 – 42

13

Beta strand

50 – 54

5

Beta strand

60 – 63

4

Helix

68 – 70

3

Beta strand

74 – 76

3

Beta strand

81 – 83

3

Helix

84 – 94

11

Beta strand

99 – 103

5

Beta strand

105 – 108

4

Helix

110 – 117

8

Beta strand

118 – 124

7

Beta strand

128 – 130

3

Helix

133 – 136

4

Helix

142 – 146

5

Beta strand

149 – 152

4

Helix

154 – 163

10

Helix

169 – 174

6

Beta strand

179 – 182

4

Helix

184 – 186

3

Helix

187 – 198

12

Helix

203 – 218

16

Helix

224 – 238

15

Helix

241 – 251

11

Sequences

	Sequence		Length	Mass (Da)
	P52045 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: B6A8A13EC2C2EBE0	FASTA	261	29,173
	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

References

	« Hide 'large scale' referencesShow '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 277:1453-1474(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.

RefSeq

NP_417394.4. NC_000913.2.
YP_491119.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EF8	X-ray	1.85	A/B/C	1-261	[»]
1EF9	X-ray	2.70	A	1-261	[»]

ProteinModelPortal

P52045.

SMR

P52045. Positions 1-261.

ModBase

Search...

Protein-protein interaction databases

STRING

511145.b2919.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC75956; AAC75956; b2919.
BAE76983; BAE76983; BAE76983.

GeneID

12930444.
947408.

KEGG

ecj:Y75_p2850.
eco:b2919.

PATRIC

32121252. VBIEscCol129921_3014.

Organism-specific databases

EchoBASE

EB2799.

EcoGene

EG12972. scpB.

Phylogenomic databases

eggNOG

COG1024.

HOGENOM

HOG000027939.

KO

K11264.

OMA

MIMSSDI.

ProtClustDB

PRK11423.

Enzyme and pathway databases

BioCyc

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

Gene expression databases

Genevestigator

P52045.

Family and domain databases

Gene3D

1.10.12.10. 1 hit.

InterPro

IPR014748. Crontonase_C.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view]

Pfam

PF00378. ECH. 1 hit.
[Graphical view]

PROSITE

PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P52045.

Entry information

Entry name

SCPB_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program