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Cite: NAR/gkaa742 2020



PUL General Information

Literature Information

PUL ID

PUL0078

PubMed

8920183, Appl Microbiol Biotechnol. 1996 Mar;45(1-2):86-93. doi: 10.1007/s002530050653.

Characterization method

enzyme activity assay

Genomic accession number

L18965.1

Nucelotide position range

1-6760

Substrate

xylan,xylose

Loci

ORF1-ORF2-xylR-xynA-ORF5-ORF6

Species

Caldicellulosiruptor sp. Rt8B.4/28238

Degradation or Biosynthesis

degradation

Gene Name

Locus Tag

Protein ID

Gene Position

GenBank Contig Range

EC Number

- - AAB42041.1 0 - 423 (+) L18965.1:1-424 -
- - AAB42042.1 455 - 1283 (+) L18965.1:456-1284 -
xylR - AAB42043.1 1370 - 2570 (+) L18965.1:1371-2571 -
xynA - AAB42044.1 2598 - 4653 (+) L18965.1:2599-4654 3.2.1.8
ORF5 - AAB42045.1 4886 - 5498 (+) L18965.1:4887-5499 -
ORF6 - AAB42046.1 5553 - 6760 (+) L18965.1:5554-6761 -

Cluster number

1

Gene name

Gene position

Gene type

Found by CGCFinder?

- 1 - 423 (+) TC: gnl|TC-DB|Q72H67|3.A.1.1.25 Yes
- 456 - 1283 (+) TC: gnl|TC-DB|G4FGN6|3.A.1.1.41 Yes
- 1371 - 2570 (+) TF: DBD-Pfam|MarR,DBD-SUPERFAMILY|0040266 Yes
- 2599 - 4653 (+) CAZyme: CBM22|GH10 Yes
- 4887 - 5498 (+) CDS No
- 5554 - 6760 (+) CDS No

PUL ID

PUL0078

PubMed

8920183, Appl Microbiol Biotechnol. 1996 Mar;45(1-2):86-93. doi: 10.1007/s002530050653.

Title

Cloning, sequencing and overexpression in Escherichia coli of a xylanase gene, xynA from the thermophilic bacterium Rt8B.4 genus Caldicellulosiruptor.

Author

Dwivedi PP, Gibbs MD, Saul DJ, Bergquist PL

Abstract

A genomic library of the extremely thermophilic eubacterial strain Rt8B.4 was constructed in lambda ZapII and screened for the expression of xylanase activity. One recombinant bacteriophage showed xylanase, xylosidase and arabinosidase activity. Sequence analysis and homology comparisons showed that this plasmid derivative, pNZ2011, was composed of 6.7 kb thermophilic DNA and contained what appeared to be an operon-like structure involving genes associated with xylose metabolism. The xylanase gene, xynA was shown to code for a multi-domain protein. Xylanase activity was shown to be associated with the carboxy-terminal domain (domain 2) by deletion analysis and also by selective polymerase chain reaction (PCR) amplification and expression of the individual domains. Denaturing polyacrylamide gel analysis of the protein encoded by the PCR product showed three main overexpressed proteins to be present in cell extracts, presumably caused by proteolytic degradation in the Escherichia coli host. The xylanase activity from domain 2 is associated with a 36-kDa protein, which is stable at 70 degrees C for at least 12 h at pH 7. The small size of this active enzymatic domain and its temperature stability suggest that it may be of value in the enzyme-enhanced bleaching of kraft pulp.