EBI Databases InterPro	Search Open in usermanual InterPro:
Jump to: InterProScan Databases Documentation FTP site Help Click on the icon for context sensitive help from the user manual. Advanced search

InterPro: IPR005192 Glycoside hydrolase, family 49

Protein matches Help

UniProtKB

Matches:

15 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
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

IPR005192 Glyco_hydro_49

Type

Family

Signatures Help

Database	ID	Name	Proteins
Pfam	PF03718	Glyco_hydro_49	15
Signatures in BioMart

InterPro Relationships Help

Contains

IPR012334 Pectin lyase fold

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.

This is a family of dextranase (EC:3.2.1.11) and isopullulanase (EC:3.2.1.57) which are all members of glycoside hydrolase family 49 (GH49). Dextranase hydrolyses alpha-1,6-glycosidic bonds in dextran polymers.

Structural links Help

PDB - click here

SCOP: b.133.1.1 , b.80.1.10

CATH: 2.160.20.10 , 2.60.350.10

Database links Help

Enzyme: EC:3.2.1

CAZy: GH49

PANDIT: PF03718

Blocks: IPB005192

CluSTr: ALLvsALL:437638:87.9

Pfam Clan: CL0268.3

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR005192

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O00105 Isopullulanase

P39652 Dextranase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR012334	Pectin lyase fold
IPR005192	Glycoside hydrolase, family 49
IPR011050	Pectin lyase fold/virulence factor
	PDB Chain
	ModBase
	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
	Akeboshi H, Kashiwagi Y, Aoki H, Tonozuka T, Nishikawa A, Sakano Y. Construction of an efficient expression system for Aspergillus isopullulanase in Pichia pastoris, and a simple purification method. Biosci. Biotechnol. Biochem. 67 2003 1149-53 [PubMed: 12834298] http://dx.doi.org/10.1271/bbb.67.1149
	Akeboshi H, Tonozuka T, Furukawa T, Ichikawa K, Aoki H, Shimonishi A, Nishikawa A, Sakano Y. Insights into the reaction mechanism of glycosyl hydrolase family 49. Site-directed mutagenesis and substrate preference of isopullulanase. Eur. J. Biochem. 271 2004 4420-7 [PubMed: 15560783] http://dx.doi.org/10.1111/j.1432-1033.2004.04378.x
	Mizuno M, Koide A, Yamamura A, Akeboshi H, Yoshida H, Kamitori S, Sakano Y, Nishikawa A, Tonozuka T. Crystal structure of Aspergillus niger isopullulanase, a member of glycoside hydrolase family 49. J. Mol. Biol. 376 2008 210-20 [PubMed: 18155243] http://dx.doi.org/10.1016/j.jmb.2007.11.098
	Larsson AM, Andersson R, Stahlberg J, Kenne L, Jones TA. Dextranase from Penicillium minioluteum: reaction course, crystal structure, and product complex. Structure 11 2003 1111-21 [PubMed: 12962629] http://dx.doi.org/10.1016/S0969-2126(03)00147-3

InterPro 23.1