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InterPro: IPR000726 Glycoside hydrolase, family 19, catalytic
Protein matches
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UniProtKB Matches: 1484 proteins |
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Accession
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IPR000726 Glyco_hydro_19_cat |
Type
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Domain |
Signatures
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InterPro Relationships
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Found in
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IPR016283 Glycoside hydrolase, family 19
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Contains
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IPR013006 Antimicrobial peptide, C6 type, conserved site
IPR018226 Barwin, conserved site
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GO Term annotation
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Process
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GO:0006032 chitin catabolic process
GO:0016998 cell wall macromolecule catabolic 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 catalyse 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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Pfam Clan: CL0037.10
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Additional Reading
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Aboitiz N, Vila-Perello M, Groves P, Asensio JL, Andreu D, Canada FJ, Jimenez-Barbero J.
NMR and modeling studies of protein-carbohydrate interactions: synthesis, three-dimensional structure, and recognition properties of a minimum hevein domain with binding affinity for chitooligosaccharides.
Chembiochem 5 2004 1245-55
[PubMed: 15368576]
http://dx.doi.org/10.1002/cbic.200400025
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Fujii T, Hayashida M, Hamasu M, Ishiguro M, Hata Y.
Structures of two lectins from the roots of pokeweed (Phytolacca americana).
Acta Crystallogr. D Biol. Crystallogr. 60 2004 665-73
[PubMed: 15039554]
http://dx.doi.org/10.1107/S090744490400232X
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Hayashida M, Fujii T, Hamasu M, Ishiguro M, Hata Y.
Similarity between protein-protein and protein-carbohydrate interactions, revealed by two crystal structures of lectins from the roots of pokeweed.
J. Mol. Biol. 334 2003 551-65
[PubMed: 14623194]
http://dx.doi.org/10.1016/j.jmb.2003.09.076
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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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Reyes-Lopez CA, Hernandez-Santoyo A, Pedraza-Escalona M, Mendoza G, Hernandez-Arana A, Rodriguez-Romero A.
Insights into a conformational epitope of Hev b 6.02 (hevein).
Biochem. Biophys. Res. Commun. 314 2004 123-30
[PubMed: 14715255]
http://dx.doi.org/10.1016/j.bbrc.2003.12.068
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InterPro 23.1
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