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InterPro: IPR001764 Glycoside hydrolase, family 3, N-terminal

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3783 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Accession

IPR001764 Glyco_hydro_3_N

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:3.20.20.300	Glyco_hydro_3_N	3665
Pfam	PF00933	Glyco_hydro_3	3764
PRINTS	PR00133	GLHYDRLASE3	2251
Signatures in BioMart

InterPro Relationships Help

Parent

IPR017853 Glycoside hydrolase, catalytic core

Contains

IPR019800 Glycoside hydrolase, family 3, active site

GO Term annotation Help

Process

GO:0005975 carbohydrate metabolic process

Function

GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds

InterPro annotation

Entry Details in BioMart

Abstract

O-Glycosyl hydrolases EC:3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [1, 2, 3]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site [4]. Because the fold of proteins is better conserved than their sequences, some of the families can be grouped in clans.

Glycoside hydrolase family 3 GH3 comprises enzymes with a number of known activities; beta-glucosidase (EC:3.2.1.21); beta-xylosidase (EC:3.2.1.37); N-acetyl beta-glucosaminidase (EC:3.2.1.52); glucan beta-1,3-glucosidase (EC:3.2.1.58); cellodextrinase (EC:3.2.1.74); exo-1,3-1,4-glucanase (EC:3.2.1). These enzymes are two-domain globular proteins that are N-glycosylated at three sites [5]. This domain is often N-terminal to the glycoside hydrolase family 3, C-terminal domain IPR002772.

Structural links Help

PDB - click here

SCOP: c.1.8.7

CATH: 3.20.20.300

Database links Help

PDBe-motif: PS00775

Enzyme: EC:3.2.1.52

CAZy: GH3

PROSITE doc: PDOC00621

PANDIT: PF00933

Blocks: IPB001764

Pfam Clan: CL0058.12

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001764

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P06835 Beta-glucosidase

P40406 Uncharacterized lipoprotein ybbD

Q23892 Lysosomal beta glucosidase

Q94KD8 Probable beta-D-xylosidase 2

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR002772	Glycoside hydrolase, family 3, C-terminal
IPR019800	Glycoside hydrolase, family 3, active site
IPR017853	Glycoside hydrolase, catalytic core
IPR001764	Glycoside hydrolase, family 3, N-terminal
	PDB Chain
	ModBase

Publications Open in usermanual
1.	Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon JP, Davies G. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc. Natl. Acad. Sci. U.S.A. 92 7090-4 1995 [PubMed: 7624375] http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=7624375&action=stream&blobtype=pdf
2.	Davies G, Henrissat B. Structures and mechanisms of glycosyl hydrolases. Structure 3 853-9 1995 [PubMed: 8535779] http://dx.doi.org/10.1016/S0969-2126(01)00220-9
3.	Bairoch A. Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT. 1999
4.	Henrissat B, Coutinho PM. Carbohydrate-Active Enzymes server. 1999
5.	Varghese JN, Hrmova M, Fincher GB. Three-dimensional structure of a barley beta-D-glucan exohydrolase, a family 3 glycosyl hydrolase. Structure 7 179-90 1999 [PubMed: 10368285] http://dx.doi.org/10.1016/S0969-2126(99)80024-0

Additional Reading Open in usermanual
	Hrmova M, Streltsov VA, Smith BJ, Vasella A, Varghese JN, Fincher GB. Structural rationale for low-nanomolar binding of transition state mimics to a family GH3 beta-D-glucan glucohydrolase from barley. Biochemistry 44 2005 16529-39 [PubMed: 16342944] http://dx.doi.org/10.1021/bi0514818
	Hrmova M, Varghese JN, De Gori R, Smith BJ, Driguez H, Fincher GB. Catalytic mechanisms and reaction intermediates along the hydrolytic pathway of a plant beta-D-glucan glucohydrolase. Structure 9 2001 1005-16 [PubMed: 11709165] http://dx.doi.org/10.1016/S0969-2126(01)00673-6
	Hrmova M, De Gori R, Smith BJ, Fairweather JK, Driguez H, Varghese JN, Fincher GB. Structural basis for broad substrate specificity in higher plant beta-D-glucan glucohydrolases. Plant Cell 14 2002 1033-52 [PubMed: 12034895] http://dx.doi.org/10.1105/tpc.010442
	Bause E, Legler G. Isolation and structure of a tryptic glycopeptide from the active site of beta-glucosidase A3 from Aspergillus wentii. Biochim. Biophys. Acta 626 1980 459-65 [PubMed: 6783081] http://dx.doi.org/10.1016/0005-2795(80)90142-7
	Hrmova M, De Gori R, Smith BJ, Vasella A, Varghese JN, Fincher GB. Three-dimensional structure of the barley beta-D-glucan glucohydrolase in complex with a transition state mimic. J. Biol. Chem. 279 2004 4970-80 [PubMed: 14597633] http://dx.doi.org/10.1074/jbc.M307188200
	Castle LA, Smith KD, Morris RO. Cloning and sequencing of an Agrobacterium tumefaciens beta-glucosidase gene involved in modifying a vir-inducing plant signal molecule. J. Bacteriol. 174 1992 1478-86 [PubMed: 1537792] http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=1537792&action=stream&blobtype=pdf

InterPro 23.1