Summary: Glycosyl hydrolase family 52
This is the Wikipedia entry entitled "Glycoside hydrolase family 52". More...
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Glycoside hydrolase family 52 Edit Wikipedia article
Glycoside 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 glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different families. This classification is available on the CAZy(http://www.cazy.org/GH1.html) web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.
Proteins harboring beta-xylosidase and xylanase activities  have been identified in the Gram-positive, facultative thermophilic aerobe Bacillus stearothermophilus 21. 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.
- Henrissat B, Callebaut I, Mornon JP, Fabrega S, Lehn P, Davies G (1995). "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases". Proc. Natl. Acad. Sci. U.S.A. 92 (15): 7090–7094. doi:10.1073/pnas.92.15.7090. PMC . PMID 7624375.
- Henrissat B, Davies G (1995). "Structures and mechanisms of glycosyl hydrolases". Structure. 3 (9): 853–859. doi:10.1016/S0969-2126(01)00220-9. PMID 8535779.
- Bairoch, A. "Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT". 1999.
- Henrissat, B. and Coutinho P.M. "Carbohydrate-Active Enzymes server". 1999.
- CAZypedia, an online encyclopedia of carbohydrate-active enzymes.
- Baba T, Shinke R, Nanmori T (July 1994). "Identification and characterization of clustered genes for thermostable xylan-degrading enzymes, beta-xylosidase and xylanase, of Bacillus stearothermophilus 21". Appl. Environ. Microbiol. 60 (7): 2252–8. PMC . PMID 8074507.
Glycosyl hydrolase family 52 Provide feedback
No Pfam abstract.
Bravman T, Zolotnitsky G, Shulami S, Belakhov V, Solomon D, Baasov T, Shoham G, Shoham Y; , FEBS Lett 2001;495:39-43.: Stereochemistry of family 52 glycosyl hydrolases: a beta-xylosidase from Bacillus stearothermophilus T-6 is a retaining enzyme. PUBMED:11322943 EPMC:11322943
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR000852
O-Glycosyl hydrolases (EC) 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 [PUBMED:7624375, PUBMED:8535779]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site.
Proteins harboring beta-xylosidase and xylanase activities [PUBMED:8074507]have been identified in the Gram-positive, facultative thermophilic aerobe Bacillus stearothermophilus 21 [PUBMED:8074507]. 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.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||xylan 1,4-beta-xylosidase activity (GO:0009044)|
|Biological process||carbohydrate metabolic process (GO:0005975)|
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
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We make a range of alignments for each Pfam-A family:
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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Curation and family details
|Number in seed:||13|
|Number in full:||54|
|Average length of the domain:||400.40 aa|
|Average identity of full alignment:||47 %|
|Average coverage of the sequence by the domain:||58.80 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 26740544 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||12|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Glyco_hydro_52 domain has been found. There are 6 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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