InterPro domain: IPR005200

General Information

  • Identifier IPR005200
  • Description Endo-1,3(4)-beta-glucanase
  • Number of genes 361
  • Gene duplication stats Loading...
  • Associated GO terms GO:0052861  

Abstract

O-Glycosyl hydrolases ( 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 ]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) website.

This is a family of beta-1,3(4)-glucanases belonging to glycoside hydrolase family 81 ( GH81 ). Proteins in this entry include fission yeast Eng1/Eng2 and budding yeast Dse4 (also known as Eng1) and Acf2. They have been shown to hydrolyse linear beta-1,3-glucan chains [ 3 ]. Eng1 is required for the degradation of the primary septum after completion of cytokinesis [ 4 , 5 ]. Eng2 may couple the endocytic coat to the actin module [ 6 ]. This entry also includes some uncharacterised proteins from plants and bacteria.


1. 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
2. Structures and mechanisms of glycosyl hydrolases. Structure 3, 853-9
3. Characterization of the endo-beta-1,3-glucanase activity of S. cerevisiae Eng2 and other members of the GH81 family. Fungal Genet. Biol. 45, 542-53
4. The endo-beta-1,3-glucanase eng1p is required for dissolution of the primary septum during cell separation in Schizosaccharomyces pombe. J. Cell. Sci. 116, 1689-98
5. Eng1p, an endo-1,3-beta-glucanase localized at the daughter side of the septum, is involved in cell separation in Saccharomyces cerevisiae. Eukaryotic Cell 1, 774-86
6. Eng2 is a component of a dynamic protein complex required for endocytic uptake in fission yeast. Traffic 15, 1122-42

Species distribution

Gene table

Loading...