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InterPro: IPR004185 Glycoside hydrolase, family 13, N-terminal Ig-like domain
Protein matches
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UniProtKB Matches: 506 proteins |
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Accession
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IPR004185 Glyco_hydro_13_lg-like_dom |
Type
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Domain |
Signatures
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InterPro Relationships
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Found in
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IPR014756 Immunoglobulin E-set
IPR017069 Maltodextrin glucosidase
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GO Term annotation
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Process
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GO:0005975 carbohydrate metabolic process
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Function
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GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
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InterPro annotation
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Entry Details in BioMart
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Abstract
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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.
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Structural links
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Database links
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Example proteins
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P38940 Neopullulanase
More proteins
Example Proteins Key
| InterPro entry accession number/name and structure databases |
Colour code |
| IPR013781 |
Glycoside hydrolase, subgroup, catalytic core |
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| IPR013780 |
Glycosyl hydrolase, family 13, all-beta |
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| IPR013783 |
Immunoglobulin-like fold |
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| IPR006589 |
Glycosyl hydrolase, family 13, subfamily, catalytic domain |
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| IPR006047 |
Glycosyl hydrolase, family 13, catalytic domain |
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| IPR017853 |
Glycoside hydrolase, catalytic core |
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| IPR004185 |
Glycoside hydrolase, family 13, N-terminal Ig-like domain |
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PDB Chain |
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ModBase |
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CATH Domain |
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SCOP Domain |
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Additional Reading
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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
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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
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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
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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
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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
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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
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