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InterPro: IPR000514 Glycoside hydrolase, family 39

Protein matchesHelp
UniProtKB
Matches:
160 proteins
AccessionHelp IPR000514 Glyco_hydro_39
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Contains IPR013781 Glycoside hydrolase, subgroup, catalytic core
GO Term annotationHelp
Process GO:0005975 carbohydrate metabolic process
Function GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
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.

Glycoside hydrolase family 39 GH39 comprises enzymes with several known activities; alpha-L-iduronidase (EC:3.2.1.76); beta-xylosidase (EC:3.2.1.37).

The most highly conserved regions in these enzymes are located in their N-terminal sections. These contain a glutamic acid residue which, on the basis of similarities with other families of glycosyl hydrolases [1], probably acts as the proton donor in their catalytic mechanism.

Structural linksHelp
SCOP: b.71.1.2 , c.1.8.3
Database linksHelp
PDBe-motif: PS01027
Enzyme: EC:3.2.1
CAZy: GH39
PROSITE doc: PDOC00787
PANDIT: PF01229
Blocks: IPB000514
Pfam Clan: CL0058.12

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR000514 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P35475 Alpha-L-iduronidase

P36906 Beta-xylosidase

P48441 Alpha-L-iduronidase

Q01634 Alpha-L-iduronidase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR008957 Fibronectin, type III-like fold
IPR013781 Glycoside hydrolase, subgroup, catalytic core
IPR017853 Glycoside hydrolase, catalytic core
IPR000514 Glycoside hydrolase, family 39
PDB Chain
ModBase
SCOP Domain
CATH Domain

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

Additional ReadingHelp
Czjzek M, Bravman T, Henrissat B, Shoham Y.
Crystallization and preliminary X-ray analysis of family 39 beta-D-xylosidase from Geobacillus stearothermophilus T-6.
Acta Crystallogr. D Biol. Crystallogr. 60 2004 583-5 [PubMed: 14993701]
http://dx.doi.org/10.1107/S0907444904001088
Yang JK, Yoon HJ, Ahn HJ, Lee BI, Pedelacq JD, Liong EC, Berendzen J, Laivenieks M, Vieille C, Zeikus GJ, Vocadlo DJ, Withers SG, Suh SW.
Crystal structure of beta-D-xylosidase from Thermoanaerobacterium saccharolyticum, a family 39 glycoside hydrolase.
J. Mol. Biol. 335 2004 155-65 [PubMed: 14659747]
http://dx.doi.org/10.1016/j.jmb.2003.10.026
Stoltzfus LJ, Sosa-Pineda B, Moskowitz SM, Menon KP, Dlott B, Hooper L, Teplow DB, Shull RM, Neufeld EF.
Cloning and characterization of cDNA encoding canine alpha-L-iduronidase. mRNA deficiency in mucopolysaccharidosis I dog.
J. Biol. Chem. 267 1992 6570-5 [PubMed: 1551868]
http://intl.jbc.org/cgi/reprint/267/10/6570.pdf
Henrissat B, Bairoch A.
New families in the classification of glycosyl hydrolases based on amino acid sequence similarities.
Biochem. J. 293 ( Pt 3) 1993 781-8 [PubMed: 8352747]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=8352747&action=stream&blobtype=pdf
Czjzek M, Ben David A, Bravman T, Shoham G, Henrissat B, Shoham Y.
Enzyme-substrate complex structures of a GH39 beta-xylosidase from Geobacillus stearothermophilus.
J. Mol. Biol. 353 2005 838-46 [PubMed: 16212978]
http://dx.doi.org/10.1016/j.jmb.2005.09.003
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InterPro 23.1