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: IPR004197 Glycoside hydrolase, family 9, N-terminal, Ig-like

Protein matches Help

UniProtKB

Matches:

165 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

IPR004197 Glyco_hydro_9_Ig-like

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF02927	CelD_N	165
Signatures in BioMart

InterPro Relationships Help

Parent

IPR014756 Immunoglobulin E-set

Found in

IPR013783 Immunoglobulin-like fold

GO Term annotation Help

Process

GO:0005975 carbohydrate metabolic process

Function

GO:0008810 cellulase activity

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.

Cellulases (Endoglucanases) EC:3.2.1.4 catalyse the endohydrolysis of 1,4-beta-D-glucosidic linkages in cellulose. This is the N-terminal ig-like domain of cellulase, enzymes containing this domain belong to family 9 of the glycoside hydrolases (GH9).

Structural links Help

PDB - click here

SCOP: b.1.18.2 , b.18.1.24

CATH: 2.60.120.360 , 2.60.40.10

Database links Help

Enzyme: EC:3.2.1

CAZy: GH9

PANDIT: PF02927

Blocks: IPB004197

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR004197

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P14090 Endoglucanase C

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR003305	Carbohydrate-binding, CenC-like
IPR007110	Immunoglobulin-like
IPR003599	Immunoglobulin subtype
IPR001701	Glycoside hydrolase, family 9
IPR013783	Immunoglobulin-like fold
IPR004197	Glycoside hydrolase, family 9, N-terminal, Ig-like
IPR014756	Immunoglobulin E-set
IPR013098	Immunoglobulin I-set
IPR012341	Six-hairpin glycosidase
IPR008928	Six-hairpin glycosidase-like
IPR008979	Galactose-binding domain-like
IPR018221	Glycoside hydrolase, family 9, active site
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

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

Additional Reading Open in usermanual
	Najmudin S, Guerreiro CI, Carvalho AL, Prates JA, Correia MA, Alves VD, Ferreira LM, Romao MJ, Gilbert HJ, Bolam DN, Fontes CM. Xyloglucan is recognized by carbohydrate-binding modules that interact with beta-glucan chains. J. Biol. Chem. 281 2006 8815-28 [PubMed: 16314409] http://dx.doi.org/10.1074/jbc.M510559200
	Dominguez R, Souchon H, Lascombe M, Alzari PM. The crystal structure of a family 5 endoglucanase mutant in complexed and uncomplexed forms reveals an induced fit activation mechanism. J. Mol. Biol. 257 1996 1042-51 [PubMed: 8632467] http://dx.doi.org/10.1006/jmbi.1996.0222
	Schubot FD, Kataeva IA, Chang J, Shah AK, Ljungdahl LG, Rose JP, Wang BC. Structural basis for the exocellulase activity of the cellobiohydrolase CbhA from Clostridium thermocellum. Biochemistry 43 2004 1163-70 [PubMed: 14756552] http://dx.doi.org/10.1021/bi030202i

InterPro 23.1