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InterPro: IPR001137 Glycoside hydrolase, family 11

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UniProtKB

Matches:

487 proteins

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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

IPR001137 Glyco_hydro_11

Type

Family

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00457	Glyco_hydro_11	487
PRINTS	PR00911	GLHYDRLASE11	469
Signatures in BioMart

InterPro Relationships Help

Contains

IPR013319 Glycoside hydrolase, family 11/12, catalytic domain
IPR018208 Glycoside hydrolase, family 11, 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 11 GH11 comprises enzymes with only one known activity, xylanase (EC:3.2.1.8). These enzymes were formerly known as cellulase family G.

Structural links Help

PDB - click here

SCOP: b.29.1.11

CATH: 2.60.120.180

Database links Help

PDBe-motif: PS00776 , PS00777

Enzyme: EC:3.2.1.8

CAZy: GH11

PROSITE doc: PDOC00622

PANDIT: PF00457

Blocks: IPB001137

Pfam Clan: CL0004.16

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001137

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O43097 Endo-1,4-beta-xylanase

O97402 Endo-1,4-beta-xylanase

P09850 Endo-1,4-beta-xylanase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR018208	Glycoside hydrolase, family 11, active site
IPR001137	Glycoside hydrolase, family 11
IPR013319	Glycoside hydrolase, family 11/12, catalytic domain
IPR008985	Concanavalin A-like lectin/glucanase
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH 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
	Vandermarliere E, Bourgois TM, Rombouts S, Van Campenhout S, Volckaert G, Strelkov SV, Delcour JA, Rabijns A, Courtin CM. Crystallographic analysis shows substrate binding at the -3 to +1 active-site subsites and at the surface of glycoside hydrolase family 11 endo-1,4-beta-xylanases. Biochem. J. 410 2008 71-9 [PubMed: 17983355] http://dx.doi.org/10.1042/BJ20071128
	Vardakou M, Dumon C, Murray JW, Christakopoulos P, Weiner DP, Juge N, Lewis RJ, Gilbert HJ, Flint JE. Understanding the structural basis for substrate and inhibitor recognition in eukaryotic GH11 xylanases. J. Mol. Biol. 375 2008 1293-305 [PubMed: 18078955] http://dx.doi.org/10.1016/j.jmb.2007.11.007
	Jiang L, Althoff EA, Clemente FR, Doyle L, Rothlisberger D, Zanghellini A, Gallaher JL, Betker JL, Tanaka F, Barbas CF 3rd, Hilvert D, Houk KN, Stoddard BL, Baker D. De novo computational design of retro-aldol enzymes. Science 319 2008 1387-91 [PubMed: 18323453] http://dx.doi.org/10.1126/science.1152692
	Jeffries TW. Biochemistry and genetics of microbial xylanases. Curr. Opin. Biotechnol. 7 1996 337-42 [PubMed: 8785441] http://dx.doi.org/10.1016/S0958-1669(96)80041-3
	Biely P, Vrsanska M, Tenkanen M, Kluepfel D. Endo-beta-1,4-xylanase families: differences in catalytic properties. J. Biotechnol. 57 1997 151-66 [PubMed: 9335171] http://dx.doi.org/10.1016/S0168-1656(97)00096-5
	Watanabe N, Akiba T, Kanai R, Harata K. Structure of an orthorhombic form of xylanase II from Trichoderma reesei and analysis of thermal displacement. Acta Crystallogr. D Biol. Crystallogr. 62 2006 784-92 [PubMed: 16790934] http://dx.doi.org/10.1107/S0907444906017379
	Miyatake H, Hasegawa T, Yamano A. New methods to prepare iodinated derivatives by vaporizing iodine labelling (VIL) and hydrogen peroxide VIL (HYPER-VIL). Acta Crystallogr. D Biol. Crystallogr. 62 2006 280-9 [PubMed: 16510975] http://dx.doi.org/10.1107/S0907444905041909
	el Hassouni M, Henrissat B, Chippaux M, Barras F. Nucleotide sequences of the arb genes, which control beta-glucoside utilization in Erwinia chrysanthemi: comparison with the Escherichia coli bgl operon and evidence for a new beta-glycohydrolase family including enzymes from eubacteria, archeabacteria, and humans. J. Bacteriol. 174 1992 765-77 [PubMed: 1732212] http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=1732212&action=stream&blobtype=pdf

InterPro 23.1