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InterPro: IPR001000 Glycoside hydrolase, family 10
Protein matches
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UniProtKB Matches: 1412 proteins |
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Accession
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IPR001000 Glyco_hydro_10 |
Type
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Family |
Signatures
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InterPro Relationships
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Contains
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IPR013781 Glycoside hydrolase, subgroup, catalytic core
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GO Term annotation
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Process
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GO:0005975 carbohydrate metabolic process
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Function
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GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
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InterPro annotation
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Entry Details in BioMart
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Abstract
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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].
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Structural links
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Database links
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Pfam Clan: CL0058.12
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Example proteins
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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 |
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| IPR001000 |
Glycoside hydrolase, family 10 |
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| IPR018289 |
MULE transposase, conserved domain |
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| IPR013781 |
Glycoside hydrolase, subgroup, catalytic core |
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| IPR007527 |
Zinc finger, SWIM-type |
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| IPR017853 |
Glycoside hydrolase, catalytic core |
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| IPR004330 |
Transcription factor, FAR1-related |
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SWISS-MODEL |
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PDB Chain |
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ModBase |
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SCOP Domain |
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CATH Domain |
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Publications
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1.
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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
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2.
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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
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3.
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Bairoch A.
Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT.
1999
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4.
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Henrissat B, Coutinho PM.
Carbohydrate-Active Enzymes server.
1999
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5.
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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
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6.
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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
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7.
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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
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8.
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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
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Additional Reading
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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
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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
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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
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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
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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
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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
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