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InterPro: IPR008265 Lipase, GDSL, active site

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Matches:

627 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

IPR008265 Lipase_GDSL_AS

Secondary

IPR001087

Type

Active_site

Signatures Help

Database	ID	Name	Proteins
PROSITE pattern	PS01098	LIPASE_GDSL_SER	627
Signatures in BioMart

InterPro Relationships Help

Found in

IPR001087 Lipase, GDSL
IPR013831 Esterase, SGNH hydrolase-type, subgroup

GO Term annotation Help

Process

GO:0006629 lipid metabolic process

Function

GO:0016298 lipase activity

InterPro annotation

Entry Details in BioMart

Abstract

A variety of lipolytic enzymes with serine as part of the active site have been identified [1]. Protein sequences which contain this active site signature include; Aeromonas hydrophila lipase, Vibrio mimicus arylesterase, Vibrio parahaemolyticus thermolabile haemolysin, rabbit phospholipase (AdRab-B), and Brassica napus anther-specific proline-rich protein. A serine has been identified as part of the active site in the A. hydrophila, V. mimicus and Escherichia coli enzymes.

Structural links Help

PDB - click here

SCOP: c.23.10.5

CATH: 3.40.50.1110

Database links Help

PDBe-motif: PS01098

Enzyme: EC:3.1.1

PROSITE doc: PDOC00842

Blocks: IPB008265

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR008265

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O54728 Phospholipase B1, membrane-associated

P0ADA1 Acyl-CoA thioesterase I

P40602 Anter-specific proline-rich protein APG

Q3TTY0 Phospholipase B1, membrane-associated

Q6P1J6 Phospholipase B1, membrane-associated

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR001087	Lipase, GDSL
IPR003882	Pistil-specific extensin-like protein
IPR013831	Esterase, SGNH hydrolase-type, subgroup
IPR008265	Lipase, GDSL, active site
IPR013830	Esterase, SGNH hydrolase-type
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Upton C, Buckley JT. A new family of lipolytic enzymes? Trends Biochem. Sci. 20 178-9 1995 [PubMed: 7610479] http://dx.doi.org/10.1016/S0968-0004(00)89002-7

Additional Reading Open in usermanual
	Lo YC, Lin SC, Shaw JF, Liaw YC. Substrate specificities of Escherichia coli thioesterase I/protease I/lysophospholipase L1 are governed by its switch loop movement. Biochemistry 44 2005 1971-9 [PubMed: 15697222] http://dx.doi.org/10.1021/bi048109x
	Lo YC, Lin SC, Shaw JF, Liaw YC. Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network. J. Mol. Biol. 330 2003 539-51 [PubMed: 12842470] http://dx.doi.org/10.1016/S0022-2836(03)00637-5

InterPro 23.1