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InterPro: IPR001000 Glycoside hydrolase, family 10

Protein matchesHelp
UniProtKB
Matches:
1412 proteins
AccessionHelp IPR001000 Glyco_hydro_10
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Contains IPR013781 Glycoside hydrolase, subgroup, catalytic core
GO Term annotationHelp
Process GO:0005975 carbohydrate metabolic process
Function GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

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 10 GH10 comprises enzymes with a number of known activities; xylanase (EC:3.2.1.8); endo-1,3-beta-xylanase (EC:3.2.1.32); cellobiohydrolase (EC:3.2.1.91). These enzymes were formerly known as cellulase family F.

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) [5, 6]. 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 F [7] or as the glycosyl hydrolases family 10 [8].

Structural linksHelp
PDB - click here
SCOP: c.1.8.3
CATH: 3.20.20.80
Database linksHelp
PDBe-motif: PS00591
Enzyme: EC:3.2.1.8
CAZy: GH10
PROSITE doc: PDOC00510
PANDIT: PF00331
Blocks: IPB001000
Pfam Clan: CL0058.12

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR001000 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O69231 Endo-1,4-beta-xylanase B

P23360 Endo-1,4-beta-xylanase

Q9LIE5 Protein FAR-RED ELONGATED HYPOCOTYL 3

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR006564 Zinc finger, PMZ-type
IPR001000 Glycoside hydrolase, family 10
IPR018289 MULE transposase, conserved domain
IPR013781 Glycoside hydrolase, subgroup, catalytic core
IPR007527 Zinc finger, SWIM-type
IPR017853 Glycoside hydrolase, catalytic core
IPR004330 Transcription factor, FAR1-related
SWISS-MODEL
PDB Chain
ModBase
SCOP Domain
CATH Domain

PublicationsHelp
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. 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
6. 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
7. 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
8. 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

Additional ReadingHelp
Ihsanawati , Kumasaka T, Kaneko T, Morokuma C, Yatsunami R, Sato T, Nakamura S, Tanaka N.
Structural basis of the substrate subsite and the highly thermal stability of xylanase 10B from Thermotoga maritima MSB8.
Proteins 61 2005 999-1009 [PubMed: 16247799]
http://dx.doi.org/10.1002/prot.20700
Manikandan K, Bhardwaj A, Gupta N, Lokanath NK, Ghosh A, Reddy VS, Ramakumar S.
Crystal structures of native and xylosaccharide-bound alkali thermostable xylanase from an alkalophilic Bacillus sp. NG-27: structural insights into alkalophilicity and implications for adaptation to polyextreme conditions.
Protein Sci. 15 2006 1951-60 [PubMed: 16823036]
http://dx.doi.org/10.1110/ps.062220206
Xie H, Flint J, Vardakou M, Lakey JH, Lewis RJ, Gilbert HJ, Dumon C.
Probing the structural basis for the difference in thermostability displayed by family 10 xylanases.
J. Mol. Biol. 360 2006 157-67 [PubMed: 16762367]
http://dx.doi.org/10.1016/j.jmb.2006.05.002
Nishimoto M, Kitaoka M, Fushinobu S, Hayashi K.
The role of conserved arginine residue in loop 4 of glycoside hydrolase family 10 xylanases.
Biosci. Biotechnol. Biochem. 69 2005 904-10 [PubMed: 15914908]
http://dx.doi.org/10.1271/bbb.69.904
Vardakou M, Flint J, Christakopoulos P, Lewis RJ, Gilbert HJ, Murray JW.
A family 10 Thermoascus aurantiacus xylanase utilizes arabinose decorations of xylan as significant substrate specificity determinants.
J. Mol. Biol. 352 2005 1060-7 [PubMed: 16140328]
http://dx.doi.org/10.1016/j.jmb.2005.07.051
Tull D, Withers SG, Gilkes NR, Kilburn DG, Warren RA, Aebersold R.
Glutamic acid 274 is the nucleophile in the active site of a "retaining" exoglucanase from Cellulomonas fimi.
J. Biol. Chem. 266 1991 15621-5 [PubMed: 1678739]
http://intl.jbc.org/cgi/reprint/266/24/15621.pdf
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InterPro 23.1