title: Cloning and sequence of a thermostable multidomain xylanase from the bacterium Rhodothermus marinus.
abstract: The gene (xyn1) encoding a Rhodothermus marinus xylanase has been cloned and expressed in Escherichia coli. The gene comprises 5 different domains in an unusual combination. The cellulose binding domains (CBDs) encoded by xyn1 are repeated in tandem at the N-terminus and show similarity with the CBD family IV. The xyn1-gene is the first example encoding a CBD family IV in combination with a xylan hydrolyzing catalytic domain of the glycosyl hydrolase family 10.
authors.affiliation: Department of Biotechnology, Center for Chemistry and Chemical Engineering, Lund University, Sweden. eva.nordberg-karlsson@biotek.lu.se
authors.forename: E
authors.initials: E
authors.lastname: Nordberg Karlsson
authors.forename: E
authors.initials: E
authors.lastname: Bartonek-Roxå
authors.forename: O
authors.initials: O
authors.lastname: Holst
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D043364:Endo-1,4-beta Xylanases; D005798:Genes, Bacterial; D006088:Gram-Negative Aerobic Bacteria / Q000201:enzymology* / Q000235:genetics; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D014995:Xylosidases / Q000235:genetics*
chemical_list: D014995:Xylosidases; D043364:Endo-1,4-beta Xylanases