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InterPro: IPR018087 Glycoside hydrolase, family 5, conserved site
Protein matches
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UniProtKB Matches: 994 proteins |
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Accession
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IPR018087 Glyco_hydro_5_CS |
Type
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Conserved_site |
Signatures
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InterPro Relationships
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Found in
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IPR001547 Glycoside hydrolase, family 5
IPR013781 Glycoside hydrolase, subgroup, catalytic core
IPR016282 Glycoside hydrolase, family 5, endoglucanase B
IPR017853 Glycoside hydrolase, 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 5 GH5 comprises enzymes with several known activities; endoglucanase (EC:3.2.1.4); beta-mannanase (EC:3.2.1.78); exo-1,3-glucanase (EC:3.2.1.58); endo-1,6-glucanase (EC:3.2.1.75); xylanase (EC:3.2.1.8); endoglycoceramidase (EC:3.2.1.123).
The microbial degradation of cellulose and xylans requires several types of enzymes. 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 A [5] or as the glycosyl hydrolases family 5 [6]. One of the conserved regions in this family contains a conserved glutamic acid residue which is potentially involved [7] in the catalytic mechanism.
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Structural links
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Database links
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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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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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6.
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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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7.
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Py B, Bortoli-German I, Haiech J, Chippaux M, Barras F.
Cellulase EGZ of Erwinia chrysanthemi: structural organization and importance of His98 and Glu133 residues for catalysis.
Protein Eng. 4 325-33 1991
[PubMed: 1677466]
http://dx.doi.org/10.1093/protein/4.3.325
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Additional Reading
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Varrot A, Davies GJ.
Direct experimental observation of the hydrogen-bonding network of a glycosidase along its reaction coordinate revealed by atomic resolution analyses of endoglucanase Cel5A.
Acta Crystallogr. D Biol. Crystallogr. 59 2003 447-52
[PubMed: 12595701]
http://dx.doi.org/10.1107/S0907444902023405
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Gloster TM, Macdonald JM, Tarling CA, Stick RV, Withers SG, Davies GJ.
Structural, thermodynamic, and kinetic analyses of tetrahydrooxazine-derived inhibitors bound to beta-glucosidases.
J. Biol. Chem. 279 2004 49236-42
[PubMed: 15356002]
http://dx.doi.org/10.1074/jbc.M407195200
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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 1991 303-15
[PubMed: 1886523]
http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=1886523
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Taylor SC, Ferguson AD, Bergeron JJ, Thomas DY.
The ER protein folding sensor UDP-glucose glycoprotein-glucosyltransferase modifies substrates distant to local changes in glycoprotein conformation.
Nat. Struct. Mol. Biol. 11 2004 128-34
[PubMed: 14730348]
http://dx.doi.org/10.1038/nsmb715
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Violot S, Aghajari N, Czjzek M, Feller G, Sonan GK, Gouet P, Gerday C, Haser R, Receveur-Brechot V.
Structure of a full length psychrophilic cellulase from Pseudoalteromonas haloplanktis revealed by X-ray diffraction and small angle X-ray scattering.
J. Mol. Biol. 348 2005 1211-24
[PubMed: 15854656]
http://dx.doi.org/10.1016/j.jmb.2005.03.026
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Baker JO, McCarley JR, Lovett R, Yu CH, Adney WS, Rignall TR, Vinzant TB, Decker SR, Sakon J, Himmel ME.
Catalytically enhanced endocellulase Cel5A from Acidothermus cellulolyticus.
Appl. Biochem. Biotechnol. 121-124 2005 129-48
[PubMed: 15917594]
http://dx.doi.org/10.1385/ABAB:121:1-3:0129
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Beguin P.
Molecular biology of cellulose degradation.
Annu. Rev. Microbiol. 44 1990 219-48
[PubMed: 2252383]
http://dx.doi.org/10.1146/annurev.mi.44.100190.001251
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InterPro 23.1
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