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InterPro: IPR003779 Carboxymuconolactone decarboxylase

Protein matches Help

UniProtKB

Matches:

3869 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR003779 CMD

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF02627	CMD	3869
Signatures in BioMart

InterPro Relationships Help

Children

IPR012788 4-carboxymuconolactone decarboxylase

Found in

IPR004674 Alkylhydroperoxidase AhpD

InterPro annotation

Entry Details in BioMart

Abstract

The catechol and protocatechuate branches of the 3-oxoadipate pathway, which are important for the bacterial degradation of aromatic compounds, converge at the common intermediate 3-oxoadipate enol-lactone. Carboxymuconolactone decarboxylase (CMD) is involved in protocatechuate catabolism. In some bacteria a gene fusion event leads to expression of CMD with a hydrolase involved in the same pathway [1].

Structural links Help

PDB - click here

SCOP: a.152.1.1 , a.152.1.2 , a.152.1.3 , a.152.1.4

CATH: 1.20.1290.10 , 1.20.5.810

Database links Help

Enzyme: EC:1.11.1.15

PANDIT: PF02627

Blocks: IPB003779

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR003779

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O74758 Uncharacterized protein C17D11.03c

P0A5N4 Alkyl hydroperoxide reductase ahpD

P47148 Uncharacterized protein YJR111C

Q58152 Uncharacterized protein MJ0742

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR003779	Carboxymuconolactone decarboxylase
IPR004675	Alkylhydroperoxidase AhpD core
IPR004674	Alkylhydroperoxidase AhpD
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Help

Eulberg D, Lakner S, Golovleva LA, Schlomann M.
Characterization of a protocatechuate catabolic gene cluster from Rhodococcus opacus 1CP: evidence for a merged enzyme with 4-carboxymuconolactone-decarboxylating and 3-oxoadipate enol-lactone-hydrolyzing activity.
J. Bacteriol. 180 1072-81 1998 [PubMed: 9495744]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=9495744&action=stream&blobtype=pdf

Additional Reading Open in usermanual
	Ito K, Arai R, Fusatomi E, Kamo-Uchikubo T, Kawaguchi S, Akasaka R, Terada T, Kuramitsu S, Shirouzu M, Yokoyama S. Crystal structure of the conserved protein TTHA0727 from Thermus thermophilus HB8 at 1.9 A resolution: A CMD family member distinct from carboxymuconolactone decarboxylase (CMD) and AhpD. Protein Sci. 15 2006 1187-92 [PubMed: 16597838] http://dx.doi.org/10.1110/ps.062148506
	Bryk R, Lima CD, Erdjument-Bromage H, Tempst P, Nathan C. Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein. Science 295 2002 1073-7 [PubMed: 11799204] http://dx.doi.org/10.1126/science.1067798
	Nunn CM, Djordjevic S, Hillas PJ, Nishida CR, Ortiz de Montellano PR. The crystal structure of Mycobacterium tuberculosis alkylhydroperoxidase AhpD, a potential target for antitubercular drug design. J. Biol. Chem. 277 2002 20033-40 [PubMed: 11914371] http://dx.doi.org/10.1074/jbc.M200864200
	Koshkin A, Nunn CM, Djordjevic S, Ortiz de Montellano PR. The mechanism of Mycobacterium tuberculosis alkylhydroperoxidase AhpD as defined by mutagenesis, crystallography, and kinetics. J. Biol. Chem. 278 2003 29502-8 [PubMed: 12761216] http://dx.doi.org/10.1074/jbc.M303747200

InterPro 23.1