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InterPro: IPR019802 Glycoside hydrolase, family 4, conserved site
Protein matches
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UniProtKB Matches: 751 proteins |
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Accession
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IPR019802 GlycHydrolase_4_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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IPR001088 Glycoside hydrolase, family 4
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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 4 GH4
comprises enzymes with several known activities; 6-phospho-beta-glucosidase (EC:3.2.1.86); 6-phospho-alpha-glucosidase (EC:3.2.1.122); alpha-galactosidase (EC:3.2.1.22).
These enzymes require NAD and a divalent ion for their activity and are proteins of about 50 kDa; e.g. 6-phospho-alpha-glucosidase requires both NAD(H) and divalent metal (Mn2+, Fe2+, Co2+, or Ni2+) for activity [5]. The signature pattern is located to a conserved region located in the central section. This region does not contain residues directly shown to be important for the catalytic activity.
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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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Thompson J, Pikis A, Ruvinov SB, Henrissat B, Yamamoto H, Sekiguchi J.
The gene glvA of Bacillus subtilis 168 encodes a metal-requiring, NAD(H)-dependent 6-phospho-alpha-glucosidase. Assignment to family 4 of the glycosylhydrolase superfamily.
J. Biol. Chem. 273 27347-56 1998
[PubMed: 9765262]
http://dx.doi.org/10.1074/jbc.273.42.27347
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Additional Reading
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Lodge JA, Maier T, Liebl W, Hoffmann V, Strater N.
Crystal structure of Thermotoga maritima alpha-glucosidase AglA defines a new clan of NAD+-dependent glycosidases.
J. Biol. Chem. 278 2003 19151-8
[PubMed: 12588867]
http://dx.doi.org/10.1074/jbc.M211626200
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Yip VL, Varrot A, Davies GJ, Rajan SS, Yang X, Thompson J, Anderson WF, Withers SG.
An unusual mechanism of glycoside hydrolysis involving redox and elimination steps by a family 4 beta-glycosidase from Thermotoga maritima.
J. Am. Chem. Soc. 126 2004 8354-5
[PubMed: 15237973]
http://dx.doi.org/10.1021/ja047632w
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Rajan SS, Yang X, Collart F, Yip VL, Withers SG, Varrot A, Thompson J, Davies GJ, Anderson WF.
Novel catalytic mechanism of glycoside hydrolysis based on the structure of an NAD+/Mn2+ -dependent phospho-alpha-glucosidase from Bacillus subtilis.
Structure 12 2004 1619-29
[PubMed: 15341727]
http://dx.doi.org/10.1016/j.str.2004.06.020
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Varrot A, Yip VL, Li Y, Rajan SS, Yang X, Anderson WF, Thompson J, Withers SG, Davies GJ.
NAD+ and metal-ion dependent hydrolysis by family 4 glycosidases: structural insight into specificity for phospho-beta-D-glucosides.
J. Mol. Biol. 346 2005 423-35
[PubMed: 15670594]
http://dx.doi.org/10.1016/j.jmb.2004.11.058
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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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