PROSITE documentation PDOC51764 [for PROSITE entry PS51764]

Glycosyl hydrolases family 26 (GH26) domain profile





Description

Glycoside hydrolases (GHs) play a critical role in both eukaryotes and prokaryotes, where they fulfill numerous important functions such as substrate acquisition and the remote remodelling of cell walls and the glycan decorations of glycoproteins. GH family 26 consists mainly of endo-β-1,4-mannanases (mannanases), although some members of this family display β-1,3-xylanase activity. The family 26 GHs are members of clan GH-A [1,2,3,4,E1].

The GH26 catalytic domain exhibits the architecture of the classical (β/α)8-barrel folding motif characteristic of a clan-GH-A member (see <PDB:2BVY>). Two Glu residues located respectively on strands β-4 and β-7 act as the catalytic acid/base and nucleophile in a double-displacement mechanism [1,2,3].

The profile we developed covers the entire GH26 domain.

Last update:

July 2015 / First entry.

Technical section

PROSITE method (with tools and information) covered by this documentation:

GH26, PS51764; Glycosyl hydrolases family 26 (GH26) domain profile  (MATRIX)


References

1AuthorsHogg D., Woo E.-J., Bolam D.N., McKie V.A., Gilbert H.J., Pickersgill R.W.
TitleCrystal structure of mannanase 26A from Pseudomonas cellulosa and analysis of residues involved in substrate binding.
SourceJ. Biol. Chem. 276:31186-31192(2001).
PubMed ID11382747
DOI10.1074/jbc.M010290200

2AuthorsLe Nours J., Anderson L., Stoll D., Stalbrand H., Lo Leggio L.
TitleThe structure and characterization of a modular endo-beta-1,4-mannanase from Cellulomonas fimi.
SourceBiochemistry 44:12700-12708(2005).
PubMed ID16171384
DOI10.1021/bi050779v

3AuthorsTaylor E.J., Goyal A., Guerreiro C.I.P.D., Prates J.A.M., Money V.A., Ferry N., Morland C., Planas A., Macdonald J.A., Stick R.V., Gilbert H.J., Fontes C.M.J.A., Davies G.J.
TitleHow family 26 glycoside hydrolases orchestrate catalysis on different polysaccharides: structure and activity of a Clostridium thermocellum lichenase, CtLic26A.
SourceJ. Biol. Chem. 280:32761-32767(2005).
PubMed ID15987675
DOI10.1074/jbc.M506580200

4AuthorsFu X., Huang X., Liu P., Lin L., Wu G., Li C., Feng C., Hong Y.
TitleCloning and characterization of a novel mannanase from Paenibacillus sp. BME-14.
SourceJ. Microbiol. Biotechnol. 20:518-524(2010).
PubMed ID20372022

E1Sourcehttp://www.cazy.org/GH26.html



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