Novel GH10 xylanase, with a fibronectin type 3 domain, from Cellulosimicrobium sp. strain HY-13, a bacterium in the gut of Eisenia fetida

Appl Environ Microbiol. 2009 Nov;75(22):7275-9. doi: 10.1128/AEM.01075-09. Epub 2009 Sep 18.

Abstract

The gene encoding a novel modular xylanase from Cellulosimicrobium sp. strain HY-13 was identified and expressed in Escherichia coli, and its truncated gene product was characterized. The enzyme consisted of three distinct functional domains, an N-terminal catalytic GH10 domain, a fibronectin type 3 domain, and C-terminal carbohydrate-binding module 2.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actinomycetales / enzymology*
  • Actinomycetales / genetics
  • Amino Acid Sequence
  • Animals
  • Endo-1,4-beta Xylanases / chemistry
  • Endo-1,4-beta Xylanases / genetics
  • Endo-1,4-beta Xylanases / metabolism
  • Fibronectins / chemistry
  • Intestines / microbiology
  • Molecular Sequence Data
  • Oligochaeta / microbiology*
  • Protein Binding
  • Protein Structure, Tertiary
  • Sequence Alignment
  • Substrate Specificity / genetics
  • Xylosidases / chemistry
  • Xylosidases / genetics
  • Xylosidases / metabolism*

Substances

  • Fibronectins
  • Xylosidases
  • Endo-1,4-beta Xylanases

Associated data

  • GENBANK/FJ859907