EBI Databases InterPro	Search Open in usermanual InterPro:
Jump to: InterProScan Databases Documentation FTP site Help Click on the icon for context sensitive help from the user manual. Advanced search

InterPro: IPR002925 Dienelactone hydrolase

Protein matches Help

UniProtKB

Matches:

2134 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

IPR002925 Dienelactn_hydro

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF01738	DLH	2134
Signatures in BioMart

GO Term annotation Help

Function

GO:0016787 hydrolase activity

InterPro annotation

Entry Details in BioMart

Abstract

Dienelactone hydrolases play a crucial role in chlorocatechol degradation via the modified ortho cleavage pathway. Enzymes induced in 4-fluorobenzoate-utilizing bacteria have been classified into three groups on the basis of their specificity towards cis- and trans-dienelactone [1]. Some proteins contain repeated small fragments of this domain (for example rat kan-1 protein).

Structural links Help

PDB - click here

SCOP: c.69.1.9

CATH: 3.40.50.1820

Database links Help

Enzyme: EC:3.1

PANDIT: PF01738

Blocks: IPB002925

Pfam Clan: CL0028.18

AC	CL0028.18
ID	AB_hydrolase
DE	Alpha/Beta hydrolase fold
PF00135	IPR002018	Carboxylesterase, type B
PF00151	IPR013818	Lipase, N-terminal
PF00326	IPR001375	Peptidase S9, prolyl oligopeptidase, catalytic domain
PF00450	IPR001563	Peptidase S10, serine carboxypeptidase
PF00561	IPR000073	Alpha/beta hydrolase fold-1
PF00756	IPR000801	Putative esterase
PF00975	IPR001031	Thioesterase
PF01083	IPR000675	Cutinase
PF01674	IPR002918	Lipase, class 2
PF01738	IPR002925	Dienelactone hydrolase
PF01764	IPR002921	Lipase, class 3
PF02089	IPR002472	Palmitoyl protein thioesterase
PF02129	IPR000383	Peptidase S15
PF02230	IPR003140	Phospholipase/carboxylesterase
PF02273	IPR003157	Acyl transferase, bacterial
PF02450	IPR003386	Lecithin:cholesterol acyltransferase
PF03096	IPR004142	Ndr
PF03403	IPR005065	Platelet-activating factor acetylhydrolase, plasma/intracellular isoform II
PF03583	IPR005152	Lipase, secreted
PF03959	IPR005645	Protein of unknown function DUF341
PF04301	IPR007398	Protein of unknown function DUF452
PF05057	IPR007751	Protein of unknown function DUF676, hydrolase-like
PF05448	IPR008391	Acetyl xylan esterase
PF05576	IPR008761	Peptidase S37, tripeptidyl aminopeptidase
PF05577	IPR008758	Peptidase S28
PF05677	IPR008536	Protein of unknown function DUF818, Chlamydia
PF05705	IPR008547	Protein of unknown function DUF829, transmembrane 53
PF05728	IPR008886	Uncharacterised protein family UPF0227
PF05990	IPR010297	Protein of unknown function DUF900, hydrolase-like
PF06028	IPR010315	Protein of unknown function DUF915, hydrolase-like
PF06057	IPR010333	Bacterial virulence
PF06259	IPR010427	Protein of unknown function DUF1023
PF06342	IPR010463	Protein of unknown function DUF1057, lipase putative
PF06500	IPR010520	Protein of unknown function DUF1100, hydrolase-like
PF06821	IPR010662	Protein of unknown function DUF1234
PF06850	IPR009656	PHB de-polymerase, C-terminal
PF07082	IPR010765	Protein of unknown function DUF1350
PF07176	IPR010802	Protein of unknown function DUF1400, cynaobacterial
PF07224	IPR010821	Chlorophyllase
PF07519	IPR011118	Tannase/feruloyl esterase
PF07819	IPR012908	PGAP1-like
PF07859	IPR013094	Alpha/beta hydrolase fold-3
PF08386	IPR013595	Peptidase S33, tripeptidyl-peptidase C-terminal
PF08538	IPR013744	Protein of unknown function DUF1749
PF08840	IPR014940	BAAT/Acyl-CoA thioester hydrolase C-terminal
PF10503	IPR010126	Esterase, PHB depolymerase

Taxonomic coverage Help

Example proteins Help

P39721 Protein AIM2

P73163 Putative carboxymethylenebutenolidase

Q09571 Uncharacterized protein K02A2.1

Q8R1G2 Carboxymethylenebutenolidase homolog

Q96DG6 Carboxymethylenebutenolidase homolog

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR002925	Dienelactone hydrolase
	ModBase

Publications Open in usermanual
1.	Schlomann M, Ngai KL, Ornston LN, Knackmuss HJ. Dienelactone hydrolase from Pseudomonas cepacia. J. Bacteriol. 175 2994-3001 1993 [PubMed: 7684040] http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=7684040&action=stream&blobtype=pdf

Additional Reading Open in usermanual
	Kim HK, Liu JW, Carr PD, Ollis DL. Following directed evolution with crystallography: structural changes observed in changing the substrate specificity of dienelactone hydrolase. Acta Crystallogr. D Biol. Crystallogr. 61 2005 920-31 [PubMed: 15983415] http://dx.doi.org/10.1107/S0907444905009042
	Robinson A, Edwards KJ, Carr PD, Barton JD, Ewart GD, Ollis DL. Structure of the C123S mutant of dienelactone hydrolase (DLH) bound with the PMS moiety of the protease inhibitor phenylmethylsulfonyl fluoride (PMSF). Acta Crystallogr. D Biol. Crystallogr. 56 2000 1376-84 [PubMed: 11053834] http://dx.doi.org/10.1107/S0907444900010647
	Pathak D, Ollis D. Refined structure of dienelactone hydrolase at 1.8 A. J. Mol. Biol. 214 1990 497-525 [PubMed: 2380986] http://dx.doi.org/10.1016/0022-2836(90)90196-S

InterPro 23.1