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InterPro: IPR006710 Glycoside hydrolase, family 43

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1966 proteins

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Accession

IPR006710 Glyco_hydro_43

Type

Family

Signatures Help

Database	ID	Name	Proteins
Pfam	PF04616	Glyco_hydro_43	1847
PANTHER	PTHR22925	Glyco_hydro_43	1717
Signatures in BioMart

InterPro Relationships Help

Children

IPR016828 Alpha-L-arabinofuranosidase
IPR016840 Glycoside hydrolase, family 43, endo-1, 5-alpha-L-arabinosidase

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.

Glycoside hydrolase family 43 GH43 includes enzymes with the following activities, beta-xylosidase (EC:3.2.1.37), alpha-L-arabinofuranosidase (EC:3.2.1.55); arabinanase (EC:3.2.1.99), and xylanase (EC:3.2.1.8).

Structural links Help

PDB - click here

SCOP: b.29.1.23 , b.67.2.1

CATH: 2.115.10.20 , 2.60.120.200

Database links Help

Enzyme: EC:3.2.1

CAZy: GH43

PANDIT: PF04616

Blocks: IPB006710

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR006710

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P42256 Arabinan endo-1,5-alpha-L-arabinosidase A

P45796 Arabinoxylan arabinofuranohydrolase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code

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
	Nurizzo D, Turkenburg JP, Charnock SJ, Roberts SM, Dodson EJ, McKie VA, Taylor EJ, Gilbert HJ, Davies GJ. Cellvibrio japonicus alpha-L-arabinanase 43A has a novel five-blade beta-propeller fold. Nat. Struct. Biol. 9 2002 665-8 [PubMed: 12198486] http://dx.doi.org/10.1038/nsb835
	Proctor MR, Taylor EJ, Nurizzo D, Turkenburg JP, Lloyd RM, Vardakou M, Davies GJ, Gilbert HJ. Tailored catalysts for plant cell-wall degradation: redesigning the exo/endo preference of Cellvibrio japonicus arabinanase 43A. Proc. Natl. Acad. Sci. U.S.A. 102 2005 2697-702 [PubMed: 15708971] http://dx.doi.org/10.1073/pnas.0500051102
	Brunzelle JS, Jordan DB, McCaslin DR, Olczak A, Wawrzak Z. Structure of the two-subsite beta-d-xylosidase from Selenomonas ruminantium in complex with 1,3-bis[tris(hydroxymethyl)methylamino]propane. Arch. Biochem. Biophys. 474 2008 157-66 [PubMed: 18374656] http://dx.doi.org/10.1016/j.abb.2008.03.007
	Yamaguchi A, Tada T, Wada K, Nakaniwa T, Kitatani T, Sogabe Y, Takao M, Sakai T, Nishimura K. Structural basis for thermostability of endo-1,5-alpha-L-arabinanase from Bacillus thermodenitrificans TS-3. J. Biochem. 137 2005 587-92 [PubMed: 15944411] http://dx.doi.org/10.1093/jb/mvi078

InterPro 23.1