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Identification of non-catalytic conserved regions in xylanases encoded by the xynB and xynD genes of the cellulolytic rumen anaerobe Ruminococcus flavefaciens
Authors:Jun-Xian Zhang  Jennifer Martin and Harry J Flint
Institution:(1) Rowett Research Institute, Greenburn Road, A132 9SB Bucksburn, Aberdeen, UK;(2) Present address: Department of Microbiology, University of Guelph, Guelph, Ontario, Canada
Abstract:xynB is one of at least four genes from the cellulolytic rumen anaerobe Ruminococcus flavefaciens 17 that encode xylanase activity. The xynB gene is predicted to encode a 781-amino acid product starting with a signal peptide, followed by an amino-terminal xylanase domain which is identical at 89% and 78% of residues, respectively, to the amino-terminal xylanase domains of the bifunctional XynD and XynA enzymes from the same organism. Two separate regions within the carboxy-terminal 537 amino acids of XynB also show close similarities with domain B of XynD. These regions show no significant homology with cellulose- or xylan-binding domains from other species, or with any other sequences, and their functions are unknown. In addition a 30 to 32-residue threonine-rich region is present in both XynD and XynB. Codon usage shows a consistent pattern of bias in the three xylanase genes from R. flavefaciens that have been sequenced.
Keywords:Xylanase  Cellulolytic bacteria  Anaerobic bacteria  Ruminococcus  Sequence conservation
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