spacer
spacer

Jump to: InterProScan Databases Documentation FTP site Help Advanced search

InterPro: IPR016283 Glycoside hydrolase, family 19

Protein matchesHelp
UniProtKB
Matches:
672 proteins
AccessionHelp IPR016283 Glyco_hydro_19
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Contains IPR000726 Glycoside hydrolase, family 19, catalytic
IPR001002 Chitin-binding, type 1
IPR018371 Chitin-binding, type 1, conserved site
GO Term annotationHelp
Process GO:0005975 carbohydrate metabolic process
Function GO:0004568 chitinase 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 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.

Structural linksHelp
SCOP: d.2.1.1 , g.3.1.1
Database linksHelp
Enzyme: EC:3.2.1.14

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR016283 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P11218 Lectin/endochitinase 1

P19171 Basic endochitinase B

Q7DNA1 Chitinase 2

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR000726 Glycoside hydrolase, family 19, catalytic
IPR001002 Chitin-binding, type 1
IPR016283 Glycoside hydrolase, family 19
IPR018371 Chitin-binding, type 1, 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. Flach J, Pilet PE, Jolles P.
What's new in chitinase research?
Experientia 48 701-16 1992 [PubMed: 1516675]
http://dx.doi.org/10.1007/BF02124285
6. Henrissat B.
A classification of glycosyl hydrolases based on amino acid sequence similarities.
Biochem. J. 280 ( Pt 2) 309-16 1991 [PubMed: 1747104]
http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=1747104

Additional ReadingHelp
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
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
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
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
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
spacer
spacer
InterPro 23.1