Nucleotide sequence of the Clostridium stercorarium xynA gene encoding xylanase A: identification of catalytic and cellulose binding domains

Biosci Biotechnol Biochem. 1993 Feb;57(2):273-7. doi: 10.1271/bbb.57.273.

Abstract

The nucleotides of the xynA gene of Clostridium stercorarium were sequenced. The structural gene consists of an open reading frame of 1533 bp encoding 511 amino acids with an M(r) of 56,519. The signal peptide cleavage site was identified by comparison with the N-terminal amino acid sequence of the enzyme produced by a recombinant Escherichia coli. Xylanase A consists of a catalytic domain belonging to family G at the N-terminus and two direct repeats of about 90 amino acids with a short spacing at the C-terminus. Deletion analysis showed that the repeated sequences were responsible for binding the enzyme to Avicel and were not essential for catalytic activity. The catalytic domain of this enzyme is highly homologous to xylanase A of Clostridium acetobutylicum (identity: 69%) and xylanase B of Bacillus pumilus (identity: 64%).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacillus / enzymology
  • Bacillus / genetics
  • Base Sequence
  • Catalysis
  • Cellulose / metabolism*
  • Cloning, Molecular
  • Clostridium / enzymology
  • Clostridium / genetics*
  • Endo-1,4-beta Xylanases
  • Escherichia coli / genetics
  • Glycoside Hydrolases / biosynthesis
  • Glycoside Hydrolases / chemistry
  • Glycoside Hydrolases / genetics*
  • Molecular Sequence Data
  • Restriction Mapping
  • Sequence Homology, Nucleic Acid

Substances

  • Cellulose
  • Glycoside Hydrolases
  • Endo-1,4-beta Xylanases

Associated data

  • GENBANK/D13325