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InterPro: IPR016283 Glycoside hydrolase, family 19
Protein matches
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UniProtKB Matches: 672 proteins |
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Accession
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IPR016283 Glyco_hydro_19 |
Type
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Family |
Signatures
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InterPro Relationships
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Contains
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IPR000726 Glycoside hydrolase, family 19, catalytic
IPR001002 Chitin-binding, type 1
IPR018371 Chitin-binding, type 1, conserved site
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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:0004568 chitinase activity
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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.
Glycoside hydrolase family 19 GH19 comprises enzymes with only one known activity; chitinase (EC:3.2.1.14).
Chitinases [5] are enzymes that catalyze the hydrolysis of the beta-1,4-N-acetyl-D-glucosamine linkages in chitin polymers. Chitinases belong to glycoside hydrolase families 18 or 19 [6]. Chitinases of family 19 (also known as classes IA or I and IB or II) are enzymes from plants that function in the defence against fungal and insect pathogens by destroying their chitin-containing cell wall. Class IA/I and IB/II enzymes differ in the presence (IA/I) or absence (IB/II) of a N-terminal chitin-binding domain. The catalytic domain of these enzymes consist of about 220 to 230 amino acid residues.
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Structural links
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Database links
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Additional Reading
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Harata K, Schubert WD, Muraki M.
Structure of Urtica dioica agglutinin isolectin I: dimer formation mediated by two zinc ions bound at the sugar-binding site.
Acta Crystallogr. D Biol. Crystallogr. 57 2001 1513-7
[PubMed: 11679714]
http://dx.doi.org/10.1107/S090744490101232X
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Saul FA, Rovira P, Boulot G, Damme EJ, Peumans WJ, Truffa-Bachi P, Bentley GA.
Crystal structure of Urtica dioica agglutinin, a superantigen presented by MHC molecules of class I and class II.
Structure 8 2000 593-603
[PubMed: 10873861]
http://dx.doi.org/10.1016/S0969-2126(00)00142-8
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Itoh Y, Kawase T, Nikaidou N, Fukada H, Mitsutomi M, Watanabe T, Itoh Y.
Functional analysis of the chitin-binding domain of a family 19 chitinase from Streptomyces griseus HUT6037: substrate-binding affinity and cis-dominant increase of antifungal function.
Biosci. Biotechnol. Biochem. 66 2002 1084-92
[PubMed: 12092819]
http://dx.doi.org/10.1271/bbb.66.1084
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Kezuka Y, Ohishi M, Itoh Y, Watanabe J, Mitsutomi M, Watanabe T, Nonaka T.
Structural studies of a two-domain chitinase from Streptomyces griseus HUT6037.
J. Mol. Biol. 358 2006 472-84
[PubMed: 16516924]
http://dx.doi.org/10.1016/j.jmb.2006.02.013
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Hahn M, Hennig M, Schlesier B, Hohne W.
Structure of jack bean chitinase.
Acta Crystallogr. D Biol. Crystallogr. 56 2000 1096-9
[PubMed: 10957628]
http://dx.doi.org/10.1107/S090744490000857X
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InterPro 23.1
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