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InterPro: IPR004185 Glycoside hydrolase, family 13, N-terminal Ig-like domain

Protein matchesHelp
UniProtKB
Matches:
506 proteins
AccessionHelp IPR004185 Glyco_hydro_13_lg-like_dom
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR014756 Immunoglobulin E-set
IPR017069 Maltodextrin glucosidase
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.

Enzymes containing this domain belong to family 13 (GH13) of the glycosyl hydrolases. The maltogenic alpha-amylase is an enzyme which catalyses hydrolysis of (1-4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the non-reducing ends of the chains in the conversion of starch to maltose. Other enzymes include neopullulanase, which hydrolyses pullulan to panose, and cyclomaltodextrinase, which hydrolyses cyclodextrins.

Structural linksHelp
SCOP: b.1.18.2 , c.1.8.1
CATH: 2.60.40.10
Database linksHelp
Enzyme: EC:3.2.1
CAZy: GH13
PANDIT: PF02903
Blocks: IPB004185

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR004185 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P38940 Neopullulanase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR013781 Glycoside hydrolase, subgroup, catalytic core
IPR013780 Glycosyl hydrolase, family 13, all-beta
IPR013783 Immunoglobulin-like fold
IPR006589 Glycosyl hydrolase, family 13, subfamily, catalytic domain
IPR006047 Glycosyl hydrolase, family 13, catalytic domain
IPR017853 Glycoside hydrolase, catalytic core
IPR004185 Glycoside hydrolase, family 13, N-terminal Ig-like domain
PDB Chain
ModBase
CATH Domain
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

Additional ReadingHelp
Ohtaki A, Mizuno M, Tonozuka T, Sakano Y, Kamitori S.
Complex structures of Thermoactinomyces vulgaris R-47 alpha-amylase 2 with acarbose and cyclodextrins demonstrate the multiple substrate recognition mechanism.
J. Biol. Chem. 279 2004 31033-40 [PubMed: 15138257]
http://dx.doi.org/10.1074/jbc.M404311200
Abe A, Tonozuka T, Sakano Y, Kamitori S.
Complex structures of Thermoactinomyces vulgaris R-47 alpha-amylase 1 with malto-oligosaccharides demonstrate the role of domain N acting as a starch-binding domain.
J. Mol. Biol. 335 2004 811-22 [PubMed: 14687576]
http://dx.doi.org/10.1016/j.jmb.2003.10.078
Kamitori S, Kondo S, Okuyama K, Yokota T, Shimura Y, Tonozuka T, Sakano Y.
Crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVAII) hydrolyzing cyclodextrins and pullulan at 2.6 A resolution.
J. Mol. Biol. 287 1999 907-21 [PubMed: 10222200]
http://dx.doi.org/10.1006/jmbi.1999.2647
Abe A, Yoshida H, Tonozuka T, Sakano Y, Kamitori S.
Complexes of Thermoactinomyces vulgaris R-47 alpha-amylase 1 and pullulan model oligossacharides provide new insight into the mechanism for recognizing substrates with alpha-(1,6) glycosidic linkages.
FEBS J. 272 2005 6145-53 [PubMed: 16302977]
http://dx.doi.org/10.1111/j.1742-4658.2005.05013.x
Ohtaki A, Mizuno M, Yoshida H, Tonozuka T, Sakano Y, Kamitori S.
Structure of a complex of Thermoactinomyces vulgaris R-47 alpha-amylase 2 with maltohexaose demonstrates the important role of aromatic residues at the reducing end of the substrate binding cleft.
Carbohydr. Res. 341 2006 1041-6 [PubMed: 16564038]
http://dx.doi.org/10.1016/j.carres.2006.01.029
Mizuno M, Tonozuka T, Uechi A, Ohtaki A, Ichikawa K, Kamitori S, Nishikawa A, Sakano Y.
The crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVA II) complexed with transglycosylated product.
Eur. J. Biochem. 271 2004 2530-8 [PubMed: 15182368]
http://dx.doi.org/10.1111/j.1432-1033.2004.04183.x
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InterPro 23.1