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InterPro: IPR000852 Glycoside hydrolase, family 52

Protein matchesHelp
UniProtKB
Matches:
20 proteins
AccessionHelp IPR000852 Glyco_hydro_52
TypeHelp Family
SignaturesHelp
GO Term annotationHelp
Process GO:0005975 carbohydrate metabolic process
Function GO:0009044 xylan 1,4-beta-xylosidase activity
InterPro annotation
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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.

Glycoside hydrolase family 52 GH52 comprises enzymes with only one known activity; beta-xylosidase (EC:3.2.1.37).

Proteins harboring beta-xylosidase and xylanase activities [5]have been identified in the Gram-positive, facultative thermophilic aerobe Bacillus stearothermophilus 21 [5]. This microbe, which functions in xylan degradation, can utilise xylan as a sole source of carbon. The enzyme hydrolyses 1,4-beta-D-xylans, removing successive D-xylose residues from the non-reducing termini. It also hydrolyses xylobiose.

Database linksHelp
CAZy: GH52
PANDIT: PF03512
Blocks: IPB000852

Taxonomic coverageHelp

Example proteinsHelp
P45702 Beta-xylosidase

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Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR000852 Glycoside hydrolase, family 52

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. Baba T, Shinke R, Nanmori T.
Identification and characterization of clustered genes for thermostable xylan-degrading enzymes, beta-xylosidase and xylanase, of Bacillus stearothermophilus 21.
Appl. Environ. Microbiol. 60 2252-8 1994 [PubMed: 8074507]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=8074507&action=stream&blobtype=pdf

Additional ReadingHelp
Bravman T, Zolotnitsky G, Shulami S, Belakhov V, Solomon D, Baasov T, Shoham G, Shoham Y.
Stereochemistry of family 52 glycosyl hydrolases: a beta-xylosidase from Bacillus stearothermophilus T-6 is a retaining enzyme.
FEBS Lett. 495 2001 39-43 [PubMed: 11322943]
http://dx.doi.org/10.1016/S0014-5793(01)02360-2
el Hassouni M, Henrissat B, Chippaux M, Barras F.
Nucleotide sequences of the arb genes, which control beta-glucoside utilization in Erwinia chrysanthemi: comparison with the Escherichia coli bgl operon and evidence for a new beta-glycohydrolase family including enzymes from eubacteria, archeabacteria, and humans.
J. Bacteriol. 174 1992 765-77 [PubMed: 1732212]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=1732212&action=stream&blobtype=pdf
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InterPro 23.1