dbCAN-PUL

Because CGCFinder predicted no CGC for this PUL, the gene cluster depicted below contains dbCAN2 and CGC signature predictions for all genes in the PUL, instead of a predicted CGC.

PUL ID	PUL0411
PubMed	7487028, Appl Environ Microbiol. 1995 Aug;61(8):2958-64. doi: 10.1128/aem.61.8.2958-2964.1995.
Characterization method	enzyme activity assay
Genomic accession number	Z49241.1
Nucelotide position range	141-2293
Substrate	xylan
Loci	XynAB
Species	Prevotella bryantii/77095
Degradation or Biosynthesis	degradation

Gene Name	Locus Tag	Protein ID	Gene Position	GenBank Contig Range	EC Number
xynA	-	CAA89207.1	141 - 1251 (+)	Z49241.1:282-1392	-
xynB	-	CAA89208.1	1333 - 2293 (+)	Z49241.1:1474-2434	-

Cluster number	0
Gene name	Gene position	Gene type	Found by CGCFinder?
-	142 - 1251 (+)	CAZyme: GH10	No
-	1334 - 2293 (+)	CAZyme: GH43_1	No

PUL ID	PUL0411
PubMed	7487028, Appl Environ Microbiol. 1995 Aug;61(8):2958-64. doi: 10.1128/aem.61.8.2958-2964.1995.
Title	A xylan hydrolase gene cluster in Prevotella ruminicola B(1)4: sequence relationships, synergistic interactions, and oxygen sensitivity of a novel enzyme with exoxylanase and beta-(1,4)-xylosidase activities.
Author	Gasparic A, Martin J, Daniel AS, Flint HJ
Abstract	Two genes concerned with xylan degradation were found to be closely linked in the ruminal anaerobe Prevotella ruminicola B(1)4, being separated by an intergenic region of 75 nucleotides. xynA is shown to encode a family F endoxylanase of 369 amino acids, including a putative amino-terminal signal peptide. xynB encodes an enzyme of 319 amino acids, with no obvious signal peptide, that shows 68% amino acid identity with the xsa product of Bacteroides ovatus and 31% amino acid identity with a beta-xylosidase from Clostridium stercorarium; together, these three enzymes define a new family of beta-(1,4)-glycosidases. The activity of the cloned P. ruminicola xynB gene product, but not that of the xynA gene product, shows considerable sensitivity to oxygen. Studied under anaerobic conditions, the XynB enzyme was found to act as an exoxylanase, releasing xylose from substrates including xylobiose, xylopentaose, and birch wood xylan, but was relatively inactive against oat spelt xylan. A high degree of synergy (up to 10-fold stimulation) was found with respect to the release of reducing sugars from oat spelt xylan when XynB was combined with the XynA endoxylanase from P. ruminicola B(1)4 or with endoxylanases from the cellulolytic rumen anaerobe Ruminococcus flavefaciens 17. Pretreatment with a fungal arabinofuranosidase also stimulated reducing-sugar release from xylans by XynB. In P. ruminicola the XynA and XynB enzymes may act sequentially in the breakdown of xylan.

Copyright 2020 © YIN LAB, UNL. All rights reserved. Designed by Catie Ausland and Jinfang Zheng. Maintained by Yanbin Yin.