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InterPro: IPR011583 Chitinase II

Protein matches Help

UniProtKB

Matches:

2647 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR011583 Chitinase_II

Secondary

IPR001223

Type

Domain

Signatures Help

Database	ID	Name	Proteins
SMART	SM00636	Glyco_18	2647
Signatures in BioMart

InterPro Relationships Help

Parent

IPR001223 Glycoside hydrolase, family 18, catalytic domain

Found in

IPR015520 Imaginal disc growth factor

Contains

IPR001579 Glycoside hydrolase, chitinase active site

GO Term annotation Help

Process

GO:0006032 chitin catabolic process

Function

GO:0004568 chitinase activity

InterPro annotation

Entry Details in BioMart

Abstract

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.

Members of this family belong to the chitinase class II group which includes chitinase, chitodextrinase and the killer toxin of Kluyveromyces lactis (Yeast) (Candida sphaerica) and all belong to glycoside hydrolase, family 18 GH18. The chitinases hydrolyse chitin oligosaccharides.

Structural links Help

PDB - click here

SCOP: c.1.8.5 , d.26.3.1

CATH: 3.10.50.10 , 3.20.20.80

Database links Help

Blocks: IPB011583

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR011583

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O35744 Chitinase-3-like protein 3

P36222 Chitinase-3-like protein 1

Q06350 Sporulation-specific chitinase 2

Q11174 Probable endochitinase

Q9V3D4 Chitinase-like protein Idgf2

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR013781	Glycoside hydrolase, subgroup, catalytic core
IPR015520	Imaginal disc growth factor
IPR017853	Glycoside hydrolase, catalytic core
IPR002557	Chitin binding protein, peritrophin-A
IPR011583	Chitinase II
IPR001579	Glycoside hydrolase, chitinase active site
IPR001223	Glycoside hydrolase, family 18, catalytic domain
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
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

Additional Reading Open in usermanual
	Ethayathulla AS, Srivastava DB, Kumar J, Saravanan K, Bilgrami S, Sharma S, Kaur P, Srinivasan A, Singh TP. Structure of the buffalo secretory signalling glycoprotein at 2.8 A resolution. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63 2007 258-65 [PubMed: 17401190]
	Kumar J, Ethayathulla AS, Srivastava DB, Singh N, Sharma S, Kaur P, Srinivasan A, Singh TP. Carbohydrate-binding properties of goat secretory glycoprotein (SPG-40) and its functional implications: structures of the native glycoprotein and its four complexes with chitin-like oligosaccharides. Acta Crystallogr. D Biol. Crystallogr. 63 2007 437-46 [PubMed: 17372347] http://dx.doi.org/10.1107/S0907444907001631
	Sharma P, Singh N, Sinha M, Sharma S, Perbandt M, Betzel C, Kaur P, Srinivasan A, Singh TP. Tryptophan as a three-way switch in regulating the function of the secretory signalling glycoprotein (SPS-40) from mammary glands: structure of SPS-40 complexed with 2-methylpentane-2,4-diol at 1.6 A resolution. Acta Crystallogr. D Biol. Crystallogr. 65 2009 375-8 [PubMed: 19307719] http://dx.doi.org/10.1107/S0907444909002327
	Andersen OA, Nathubhai A, Dixon MJ, Eggleston IM, van Aalten DM. Structure-based dissection of the natural product cyclopentapeptide chitinase inhibitor argifin. Chem. Biol. 15 2008 295-301 [PubMed: 18355729] http://dx.doi.org/10.1016/j.chembiol.2008.02.015
	Srivastava DB, Ethayathulla AS, Kumar J, Somvanshi RK, Sharma S, Dey S, Singh TP. Carbohydrate binding properties and carbohydrate induced conformational switch in sheep secretory glycoprotein (SPS-40): crystal structures of four complexes of SPS-40 with chitin-like oligosaccharides. J. Struct. Biol. 158 2007 255-66 [PubMed: 17188513] http://dx.doi.org/10.1016/j.jsb.2006.11.002

InterPro 23.1