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InterPro: IPR013739 Beta-galactosidase C-terminal
Protein matches
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UniProtKB Matches: 365 proteins |
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Accession
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IPR013739 Beta_Galactosidase_C |
Type
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Domain |
Signatures
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InterPro Relationships
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Found in
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IPR003476 Glycoside hydrolase, family 42
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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.
This domain is found at the C terminus of beta-galactosidase enzymes that belong to the glycosyl hydrolase 42 family [5].
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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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Hidaka M, Fushinobu S, Ohtsu N, Motoshima H, Matsuzawa H, Shoun H, Wakagi T.
Trimeric crystal structure of the glycoside hydrolase family 42 beta-galactosidase from Thermus thermophilus A4 and the structure of its complex with galactose.
J. Mol. Biol. 322 79-91 2002
[PubMed: 12215416]
http://dx.doi.org/10.1016/S0022-2836(02)00746-5
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InterPro 23.1
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