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InterPro: IPR016840 Glycoside hydrolase, family 43, endo-1, 5-alpha-L-arabinosidase

Protein matchesHelp
UniProtKB
Matches:
124 proteins
AccessionHelp IPR016840 Glyco_hydro_43_endo_a_Ara-ase
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR006710 Glycoside hydrolase, family 43
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 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).

This entry represents an endo-1,5-alpha-L-arabinosidase.

Structural linksHelp
SCOP: b.67.2.1
CATH: 2.115.10.20

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR016840 Numbers of overlapping proteins Average numbers of overlapping amino acids

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

P94522 Arabinan endo-1,5-alpha-L-arabinosidase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR016840 Glycoside hydrolase, family 43, endo-1, 5-alpha-L-arabinosidase
IPR006710 Glycoside hydrolase, family 43
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

Additional ReadingHelp
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
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
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InterPro 23.1