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InterPro: IPR005154 Glycoside hydrolase family 67

Protein matchesHelp
UniProtKB
Matches:
104 proteins
AccessionHelp IPR005154 Glyco_hydro_67
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR011395 Alpha-glucuronidase
GO Term annotationHelp
Process GO:0045493 xylan catabolic process
Function GO:0046559 alpha-glucuronidase activity
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.

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].

Structural linksHelp
SCOP: d.92.2.2
CATH: 3.30.379.10
Database linksHelp
Enzyme: EC:3.2.1.139
CAZy: GH67
PANDIT: PF03648
Blocks: IPB005154

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR005154 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O42814 Alpha-glucuronidase

P96105 Alpha-glucuronidase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR013781 Glycoside hydrolase, subgroup, catalytic core
IPR005154 Glycoside hydrolase family 67
IPR017853 Glycoside hydrolase, catalytic core
IPR011395 Alpha-glucuronidase
IPR011100 Glycosyl hydrolase 67 middle
IPR011099 Glycosyl hydrolase 67, C-terminal
SWISS-MODEL
ModBase

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
5. 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

Additional ReadingHelp
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
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
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