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InterPro: IPR002037 Glycoside hydrolase, family 8

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UniProtKB

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478 proteins

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Accession

IPR002037 Glyco_hydro_8

Type

Family

Signatures Help

Database	ID	Name	Proteins
Pfam	PF01270	Glyco_hydro_8	478
PRINTS	PR00735	GLHYDRLASE8	446
Signatures in BioMart

InterPro Relationships Help

Contains

IPR012341 Six-hairpin glycosidase
IPR019834 Glycoside hydrolase, family 8, conserved 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 8 GH8 comprises enzymes with several known activities; endoglucanase (EC:3.2.1.4); lichenase (EC:3.2.1.73); chitosanase (EC:3.2.1.132). These enzymes were formerly known as cellulase family D [5].

Structural links Help

PDB - click here

SCOP: a.102.1.2

CATH: 1.50.10.10

Database links Help

PDBe-motif: PS00812

Enzyme: EC:3.2.1.4

CAZy: GH8

PROSITE doc: PDOC00640

PANDIT: PF01270

Blocks: IPB002037

Pfam Clan: CL0059.11

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR002037

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A3DC29 Endoglucanase A

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR016134	Cellulosome enzyme, dockerin type I
IPR019834	Glycoside hydrolase, family 8, conserved site
IPR012341	Six-hairpin glycosidase
IPR008928	Six-hairpin glycosidase-like
IPR018247	EF-Hand 1, calcium-binding site
IPR002105	Cellulosome enzyme, dockerin type I, calcium-binding motif
IPR002037	Glycoside hydrolase, family 8
IPR018242	Dockerin type 1
	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
5.	Henrissat B, Claeyssens M, Tomme P, Lemesle L, Mornon JP. Cellulase families revealed by hydrophobic cluster analysis. Gene 81 83-95 1989 [PubMed: 2806912] http://dx.doi.org/10.1016/0378-1119(89)90339-9

Additional Reading Open in usermanual
	Adachi W, Sakihama Y, Shimizu S, Sunami T, Fukazawa T, Suzuki M, Yatsunami R, Nakamura S, Takenaka A. Crystal structure of family GH-8 chitosanase with subclass II specificity from Bacillus sp. K17. J. Mol. Biol. 343 2004 785-95 [PubMed: 15465062] http://dx.doi.org/10.1016/j.jmb.2004.08.028
	Yasutake Y, Kawano S, Tajima K, Yao M, Satoh Y, Munekata M, Tanaka I. Structural characterization of the Acetobacter xylinum endo-beta-1,4-glucanase CMCax required for cellulose biosynthesis. Proteins 64 2006 1069-77 [PubMed: 16804941] http://dx.doi.org/10.1002/prot.21052
	Alzari PM, Souchon H, Dominguez R. The crystal structure of endoglucanase CelA, a family 8 glycosyl hydrolase from Clostridium thermocellum. Structure 4 1996 265-75 [PubMed: 8805535] http://dx.doi.org/10.1016/S0969-2126(96)00031-7
	De Vos D, Collins T, Nerinckx W, Savvides SN, Claeyssens M, Gerday C, Feller G, Van Beeumen J. Oligosaccharide binding in family 8 glycosidases: crystal structures of active-site mutants of the beta-1,4-xylanase pXyl from Pseudoaltermonas haloplanktis TAH3a in complex with substrate and product. Biochemistry 45 2006 4797-807 [PubMed: 16605248] http://dx.doi.org/10.1021/bi052193e
	Collins T, De Vos D, Hoyoux A, Savvides SN, Gerday C, Van Beeumen J, Feller G. Study of the active site residues of a glycoside hydrolase family 8 xylanase. J. Mol. Biol. 354 2005 425-35 [PubMed: 16246370] http://dx.doi.org/10.1016/j.jmb.2005.09.064
	Fushinobu S, Hidaka M, Honda Y, Wakagi T, Shoun H, Kitaoka M. Structural basis for the specificity of the reducing end xylose-releasing exo-oligoxylanase from Bacillus halodurans C-125. J. Biol. Chem. 280 2005 17180-6 [PubMed: 15718242] http://dx.doi.org/10.1074/jbc.M413693200

InterPro 23.1