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InterPro: IPR013831 Esterase, SGNH hydrolase-type, subgroup

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4600 proteins

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Accession

IPR013831 Esterase_SGNH_hydro-type_subgr

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:3.40.50.1110	Esterase_SGNH_hydro-type_subgr	4600
Signatures in BioMart

InterPro Relationships Help

Parent

IPR013830 Esterase, SGNH hydrolase-type

Found in

IPR001087 Lipase, GDSL
IPR007407 Protein of unknown function DUF459

Contains

IPR008265 Lipase, GDSL, active site

GO Term annotation Help

Function

GO:0016787 hydrolase activity

InterPro annotation

Entry Details in BioMart

Abstract

This entry represents a subgroup of the SGNH hydrolase-type esterase domain, which has a similar fold to flavoproteins, namely a three-layer alpha/beta/alpha structure, where the beta-sheets are composed of five parallel strands. Enzymes containing this domain act as esterases and lipases, but have little sequence homology to true lipases [1]. Proteins containing this type of esterase domain have been found in a variety of hydrolases; those with structural information include an esterase from Streptomyces scabies [2]; mammalian acetylhydrolases [3]; fungal rhamnogalacturonan acetylesterase [4]; and the multifunctional enzyme thioesterase I (TAP) from Escherichia coli [5]. SGNH hydrolase-type esterase domains contain unique hydrogen bond network that stabilises their catalytic centres; they usually contain the catalytic triad Ser/Acid/His.

Structural links Help

PDB - click here

SCOP: a.48.1.1 , c.23.10.1 , c.23.10.3 , c.23.10.4 , c.23.10.5 , c.23.10.6 , c.23.10.8 , c.23.10.9

CATH: 1.20.930.20 , 3.40.50.1110

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR013831

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O80443 GDSL esterase/lipase At2g38180

P41734 Isoamyl acetate-hydrolyzing esterase

P68402 Platelet-activating factor acetylhydrolase IB subunit beta

Q61205 Platelet-activating factor acetylhydrolase IB subunit gamma

Q9VXP4 Platelet-activating factor acetylhydrolase IB subunit beta homolog

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR001087	Lipase, GDSL
IPR013831	Esterase, SGNH hydrolase-type, subgroup
IPR013830	Esterase, SGNH hydrolase-type
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Akoh CC, Lee GC, Liaw YC, Huang TH, Shaw JF. GDSL family of serine esterases/lipases. Prog. Lipid Res. 43 534-52 2004 [PubMed: 15522763] http://dx.doi.org/10.1016/j.plipres.2004.09.002
2.	Wei Y, Schottel JL, Derewenda U, Swenson L, Patkar S, Derewenda ZS. A novel variant of the catalytic triad in the Streptomyces scabies esterase. Nat. Struct. Biol. 2 218-23 1995 [PubMed: 7773790] http://dx.doi.org/10.1038/nsb0395-218
3.	Sheffield PJ, McMullen TW, Li J, Ho YS, Garrard SM, Derewenda U, Derewenda ZS. Preparation and crystal structure of the recombinant alpha(1)/alpha(2) catalytic heterodimer of bovine brain platelet-activating factor acetylhydrolase Ib. Protein Eng. 14 513-9 2001 [PubMed: 11522926] http://dx.doi.org/10.1093/protein/14.7.513
4.	Molgaard A, Larsen S. A branched N-linked glycan at atomic resolution in the 1.12 A structure of rhamnogalacturonan acetylesterase. Acta Crystallogr. D Biol. Crystallogr. 58 111-9 2002 [PubMed: 11752785]
5.	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. 330 539-51 2003 [PubMed: 12842470] http://dx.doi.org/10.1016/S0022-2836(03)00637-5

Additional Reading Open in usermanual
	Molgaard A, Larsen S. Crystal packing in two pH-dependent crystal forms of rhamnogalacturonan acetylesterase. Acta Crystallogr. D Biol. Crystallogr. 60 2004 472-8 [PubMed: 14993671] http://dx.doi.org/10.1107/S0907444903029767
	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
	Tarricone C, Perrina F, Monzani S, Massimiliano L, Kim MH, Derewenda ZS, Knapp S, Tsai LH, Musacchio A. Coupling PAF signaling to dynein regulation: structure of LIS1 in complex with PAF-acetylhydrolase. Neuron 44 2004 809-21 [PubMed: 15572112] http://dx.doi.org/10.1016/j.neuron.2004.11.019

InterPro 23.1