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InterPro: IPR000490 Glycoside hydrolase, family 17

Protein matchesHelp
UniProtKB
Matches:
1359 proteins
AccessionHelp IPR000490 Glyco_hydro_17
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 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.

Structural linksHelp
SCOP: c.1.8.3
CATH: 3.20.20.80
Database linksHelp
PDBe-motif: PS00587
Enzyme: EC:3.2.1.39
CAZy: GH17
PROSITE doc: PDOC00507
PANDIT: PF00332
Blocks: IPB000490
Pfam Clan: CL0058.12

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR000490 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O13990 Glucan 1,3-beta-glucosidase

O65399 Glucan endo-1,3-beta-glucosidase 1

P15703 Glucan 1,3-beta-glucosidase

P15737 Glucan endo-1,3-beta-glucosidase GII

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR000490 Glycoside hydrolase, family 17
IPR013781 Glycoside hydrolase, subgroup, catalytic core
IPR012946 X8
IPR017853 Glycoside hydrolase, catalytic core
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

Additional ReadingHelp
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
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
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
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
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