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InterPro: IPR018208 Glycoside hydrolase, family 11, active site

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UniProtKB

Matches:

438 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

IPR018208 Glyco_hydro_11_AS

Type

Active_site

Signatures Help

Database	ID	Name	Proteins
PROSITE pattern	PS00776	GLYCOSYL_HYDROL_F11_1	422
PROSITE pattern	PS00777	GLYCOSYL_HYDROL_F11_2	285
Signatures in BioMart

InterPro Relationships Help

Found in

IPR001137 Glycoside hydrolase, family 11
IPR008985 Concanavalin A-like lectin/glucanase
IPR013319 Glycoside hydrolase, family 11/12, catalytic domain

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

The microbial degradation of cellulose and xylans requires several types of enzymes such as endoglucanases (EC:3.2.1.4), cellobiohydrolases (EC:3.2.1.91) (exoglucanases), or xylanases (EC:3.2.1.8) [1, 2]. Fungi and bacteria produces a spectrum of cellulolytic enzymes (cellulases) and xylanases which, on the basis of sequence similarities, can be classified into families. One of these families is known as the cellulase family G [3] or as the glycosyl hydrolases family 11 [4].

The two patterns in this entry are conserved regions in these enzymes and are centred on glutamic acid residues which have both been shown [5], in Bacillus pumilis xylanase, to be necessary for catalytic activity.

Structural links Help

PDB - click here

SCOP: b.29.1.11

CATH: 2.60.120.180

Database links Help

Enzyme: EC:3.2.1.8

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR018208

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.	Beguin P. Molecular biology of cellulose degradation. Annu. Rev. Microbiol. 44 219-48 1990 [PubMed: 2252383] http://dx.doi.org/10.1146/annurev.mi.44.100190.001251
2.	Gilkes NR, Henrissat B, Kilburn DG, Miller RC Jr, Warren RA. Domains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families. Microbiol. Rev. 55 303-15 1991 [PubMed: 1886523] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=1886523
3.	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
4.	Henrissat B. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 280 ( Pt 2) 309-16 1991 [PubMed: 1747104] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=1747104
5.	Ko EP, Akatsuka H, Moriyama H, Shinmyo A, Hata Y, Katsube Y, Urabe I, Okada H. Site-directed mutagenesis at aspartate and glutamate residues of xylanase from Bacillus pumilus. Biochem. J. 288 ( Pt 1) 117-21 1992 [PubMed: 1359880] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=1359880

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
	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

InterPro 23.1