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InterPro: IPR005196 Glycoside hydrolase family 65, N-terminal
Protein matches
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UniProtKB Matches: 611 proteins |
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Accession
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IPR005196 Glyco_hydro_65_N |
Type
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Domain |
Signatures
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InterPro Relationships
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Parent
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IPR011013 Glycoside hydrolase-type carbohydrate-binding
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Found in
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IPR017045 Maltose phosphorylase/glycosyl hydrolase/vacuolar acid trehalase
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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:0003824 catalytic activity
GO:0030246 carbohydrate binding
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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.
The family of glycosyl hydrolases (GH65) containing this domain includes vacuolar acid trehalase and maltose phosphorylase. Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucose. This domain is believed to be essential for catalytic activity [5] although its precise function remains unknown.
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Structural links
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Database links
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Pfam Clan: CL0103.8
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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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Egloff MP, Uppenberg J, Haalck L, van Tilbeurgh H.
Crystal structure of maltose phosphorylase from Lactobacillus brevis: unexpected evolutionary relationship with glucoamylases.
Structure 9 689-97 2001
[PubMed: 11587643]
http://dx.doi.org/10.1016/S0969-2126(01)00626-8
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InterPro 23.1
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