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InterPro: IPR005154 Glycoside hydrolase family 67
Protein matches
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UniProtKB Matches: 104 proteins |
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Accession
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IPR005154 Glyco_hydro_67 |
Type
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Domain |
Signatures
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InterPro Relationships
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Found in
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IPR011395 Alpha-glucuronidase
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GO Term annotation
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Process
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GO:0045493 xylan catabolic process
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Function
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GO:0046559 alpha-glucuronidase activity
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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 represents a family of alpha-glucuronidases (GH67). Deletion mutants have indicated that the central region is responsible for the catalytic activity. Within this central domain, the invariant Glu and Asp (residues 391 and 364 respectively from Bacillus stearothermophilus (Geobacillus stearothermophilus)) are thought to from the the catalytic centre [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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Zaide G, Shallom D, Shulami S, Zolotnitsky G, Golan G, Baasov T, Shoham G, Shoham Y.
Biochemical characterization and identification of catalytic residues in alpha-glucuronidase from Bacillus stearothermophilus T-6.
Eur. J. Biochem. 268 3006-16 2001
[PubMed: 11358519]
http://dx.doi.org/10.1046/j.1432-1327.2001.02193.x
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Additional Reading
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Nagy T, Nurizzo D, Davies GJ, Biely P, Lakey JH, Bolam DN, Gilbert HJ.
The alpha-glucuronidase, GlcA67A, of Cellvibrio japonicus utilizes the carboxylate and methyl groups of aldobiouronic acid as important substrate recognition determinants.
J. Biol. Chem. 278 2003 20286-92
[PubMed: 12654910]
http://dx.doi.org/10.1074/jbc.M302205200
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Nurizzo D, Nagy T, Gilbert HJ, Davies GJ.
The structural basis for catalysis and specificity of the Pseudomonas cellulosa alpha-glucuronidase, GlcA67A.
Structure 10 2002 547-56
[PubMed: 11937059]
http://dx.doi.org/10.1016/S0969-2126(02)00742-6
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Golan G, Shallom D, Teplitsky A, Zaide G, Shulami S, Baasov T, Stojanoff V, Thompson A, Shoham Y, Shoham G.
Crystal structures of Geobacillus stearothermophilus alpha-glucuronidase complexed with its substrate and products: mechanistic implications.
J. Biol. Chem. 279 2004 3014-24
[PubMed: 14573597]
http://dx.doi.org/10.1074/jbc.M310098200
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InterPro 23.1
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