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InterPro: IPR001223 Glycoside hydrolase, family 18, catalytic domain

Protein matches Help

UniProtKB

Matches:

4831 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

IPR001223 Glyco_hydro18cat

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00704	Glyco_hydro_18	4831
Signatures in BioMart

InterPro Relationships Help

Parent

IPR013781 Glycoside hydrolase, subgroup, catalytic core

Children

IPR011583 Chitinase II

Found in

IPR000677 2S globulin
IPR016289 Glycoside hydrolase, family 18, endo-beta-N-acetylglucosaminidase

Contains

IPR001579 Glycoside hydrolase, chitinase active site

GO Term annotation Help

Process

GO:0005975 carbohydrate metabolic process

Function

GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds

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.

Some members of this family, GH18, belong to the chitinase class II group which includes chitinase, chitodextrinase and the killer toxin of Kluyveromyces lactis. The chitinases hydrolyse chitin oligosaccharides. The family also includes various glycoproteins from mammals; cartilage glycoprotein and the oviduct-specific glycoproteins are two examples.

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

CAZy: GH18

PANDIT: PF00704

Blocks: IPB001223

Pfam Clan: CL0058.12

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001223

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O35744 Chitinase-3-like protein 3

P29029 Endochitinase

P36222 Chitinase-3-like protein 1

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
IPR005089	Glycoside hydrolase, family 18, carbohydrate-binding
IPR001579	Glycoside hydrolase, chitinase active site
IPR017853	Glycoside hydrolase, catalytic core
IPR002557	Chitin binding protein, peritrophin-A
IPR011583	Chitinase II
IPR001223	Glycoside hydrolase, family 18, catalytic domain
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP 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
	Perrakis A, Tews I, Dauter Z, Oppenheim AB, Chet I, Wilson KS, Vorgias CE. Crystal structure of a bacterial chitinase at 2.3 A resolution. Structure 2 1994 1169-80 [PubMed: 7704527] http://dx.doi.org/10.1016/S0969-2126(94)00119-7
	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]
	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
	Hurtado-Guerrero R, van Aalten DM. Structure of Saccharomyces cerevisiae chitinase 1 and screening-based discovery of potent inhibitors. Chem. Biol. 14 2007 589-99 [PubMed: 17524989] http://dx.doi.org/10.1016/j.chembiol.2007.03.015

InterPro 23.1