spacer
spacer

Jump to: InterProScan Databases Documentation FTP site Help Advanced search

InterPro: IPR000726 Glycoside hydrolase, family 19, catalytic

Protein matchesHelp
UniProtKB
Matches:
1484 proteins
AccessionHelp IPR000726 Glyco_hydro_19_cat
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR016283 Glycoside hydrolase, family 19
Contains IPR013006 Antimicrobial peptide, C6 type, conserved site
IPR018226 Barwin, conserved site
GO Term annotationHelp
Process GO:0006032 chitin catabolic process
GO:0016998 cell wall macromolecule catabolic 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 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.

Structural linksHelp
Database linksHelp
PDBe-motif: PS00773 , PS00774
CAZy: GH19
PROSITE doc: PDOC00620
PANDIT: PF00182
Blocks: IPB000726
Pfam Clan: CL0037.10

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR000726 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P02876 Agglutinin isolectin 2

P19171 Basic endochitinase B

P44187 Uncharacterized protein HI1415

P73455 Uncharacterized protein ssl3177

Q7DNA1 Chitinase 2

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR000726 Glycoside hydrolase, family 19, catalytic
IPR001153 Barwin
IPR016283 Glycoside hydrolase, family 19
IPR001002 Chitin-binding, type 1
IPR018371 Chitin-binding, type 1, conserved site
IPR005132 Rare lipoprotein A
IPR009009 Barwin-related endoglucanase
SWISS-MODEL
PDB Chain
ModBase
SCOP Domain
CATH 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
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
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
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
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
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
spacer
spacer
InterPro 23.1