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InterPro: IPR002772 Glycoside hydrolase, family 3, C-terminal

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2435 proteins

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

IPR002772 Glyco_hydro_3_C

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF01915	Glyco_hydro_3_C	2416
SuperFamily	SSF52279	Glyco_hydro_3_C	2337
Signatures in BioMart

InterPro Relationships Help

Contains

IPR011658 PA14

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

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 [1]. This domain is often C-terminal to the glycoside hydrolase family 3, N-terminal domain IPR001764.

Structural links Help

PDB - click here

SCOP: c.23.11.1

CATH: 3.40.50.1700

Database links Help

Enzyme: EC:3.2.1

PANDIT: PF01915

Blocks: IPB002772

Taxonomic coverage Help

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.	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
	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

InterPro 23.1