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InterPro: IPR000490 Glycoside hydrolase, family 17
Protein matches
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UniProtKB Matches: 1359 proteins |
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Accession
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IPR000490 Glyco_hydro_17 |
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 17 GH17 comprises enzymes with several known activities; endo-1,3-beta-glucosidase (EC:3.2.1.39); lichenase (EC:3.2.1.73); exo-1,3-glucanase (EC:3.2.1.58). Currently these enzymes have only been found in plants and in fungi.
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Structural links
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Database links
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Pfam Clan: CL0058.12
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Additional Reading
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Muller JJ, Thomsen KK, Heinemann U.
Crystal structure of barley 1,3-1,4-beta-glucanase at 2.0-A resolution and comparison with Bacillus 1,3-1,4-beta-glucanase.
J. Biol. Chem. 273 1998 3438-46
[PubMed: 9452466]
http://dx.doi.org/10.1074/jbc.273.6.3438
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Receveur-Brechot V, Czjzek M, Barre A, Roussel A, Peumans WJ, Van Damme EJ, Rouge P.
Crystal structure at 1.45-A resolution of the major allergen endo-beta-1,3-glucanase of banana as a molecular basis for the latex-fruit syndrome.
Proteins 63 2006 235-42
[PubMed: 16421930]
http://dx.doi.org/10.1002/prot.20876
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Varghese JN, Garrett TP, Colman PM, Chen L, Hoj PB, Fincher GB.
Three-dimensional structures of two plant beta-glucan endohydrolases with distinct substrate specificities.
Proc. Natl. Acad. Sci. U.S.A. 91 1994 2785-9
[PubMed: 8146192]
http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=8146192
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Ori N, Sessa G, Lotan T, Himmelhoch S, Fluhr R.
A major stylar matrix polypeptide (sp41) is a member of the pathogenesis-related proteins superclass.
EMBO J. 9 1990 3429-36
[PubMed: 2120041]
http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=2120041
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Henrissat B.
A classification of glycosyl hydrolases based on amino acid sequence similarities.
Biochem. J. 280 ( Pt 2) 1991 309-16
[PubMed: 1747104]
http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=1747104
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InterPro 23.1
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