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InterPro: IPR001661 Glycoside hydrolase, family 37

Protein matchesHelp
UniProtKB
Matches:
681 proteins
AccessionHelp IPR001661 Glyco_hydro_37
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Contains IPR008928 Six-hairpin glycosidase-like
IPR018232 Glycoside hydrolase, family 37, conserved site
GO Term annotationHelp
Process GO:0005991 trehalose metabolic process
Function GO:0004555 alpha,alpha-trehalase 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.

Glycoside hydrolase family 37 GH37 comprises enzymes with only one known activity; trehalase (EC:3.2.1.28).

Trehalase is the enzyme responsible for the degradation of the disaccharide alpha,alpha-trehalose yielding two glucose subunits [5]. It is an enzyme found in a wide variety of organisms and whose sequence has been highly conserved throughout evolution.

Structural linksHelp
SCOP: a.102.1.9
Database linksHelp
PDBe-motif: PS00927 , PS00928
Enzyme: EC:3.2.1.28
CAZy: GH37
PROSITE doc: PDOC00717
PANDIT: PF01204
Blocks: IPB001661
Pfam Clan: CL0211.5

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR001661 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O43280 Trehalase

P13482 Periplasmic trehalase

P32356 Neutral trehalase

Q9JLT2 Trehalase

Q9W2M2 Trehalase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR008928 Six-hairpin glycosidase-like
IPR011120 Neutral trehalase Ca2+ binding
IPR001661 Glycoside hydrolase, family 37
IPR018232 Glycoside hydrolase, family 37, conserved site
SWISS-MODEL
PDB Chain
ModBase
SCOP 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
5. Kopp M, Muller H, Holzer H.
Molecular analysis of the neutral trehalase gene from Saccharomyces cerevisiae.
J. Biol. Chem. 268 4766-74 1993 [PubMed: 8444853]
http://intl.jbc.org/cgi/reprint/268/7/4766.pdf

Additional ReadingHelp
Gibson RP, Gloster TM, Roberts S, Warren RA, Storch de Gracia I, Garcia A, Chiara JL, Davies GJ.
Molecular basis for trehalase inhibition revealed by the structure of trehalase in complex with potent inhibitors.
Angew. Chem. Int. Ed. Engl. 46 2007 4115-9 [PubMed: 17455176]
Voit EO.
Biochemical and genomic regulation of the trehalose cycle in yeast: review of observations and canonical model analysis.
J. Theor. Biol. 223 2003 55-78 [PubMed: 12782117]
http://dx.doi.org/10.1016/S0022-5193(03)00072-9
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InterPro 23.1