title: Genes for D-arabinitol and ribitol catabolism from Klebsiella pneumoniae.
abstract: The enzymes for catabolism of the pentitols D-arabinitol (Dal) and ribitol (Rbt) and the corresponding genes from Klebsiella pneumoniae (dal and rbt) and Escherichia coli (atl and rtl) have been used intensively in experimental evolutionary studies. Four dal and four rbt genes from the chromosome of K. pneumoniae 1033-5P14 were cloned and sequenced. These genes are clustered in two adjacent but divergently transcribed operons and separated by two convergently transcribed repressor genes, dalR and rbtR. Each operon encodes an NAD-dependent pentose dehydrogenase (dalD and rbtD), and ATP-dependent pentulose kinase (dalK and rbtK) and a pentose-specific ion symporter (dalT and rbtT). Although the biochemical reactions which they catalyse are highly similar, the enzymes showed interesting deviations. Thus, DalR (313 aa) and RbtR (270 aa) belong to different repressor families, and DalD (455 aa) and RbtD (248 aa), which are active as a monomer or as tetramers, respectively, belong to different dehydrogenase families. Of the two kinases (19.3% identity), DalK (487 aa) belongs to the subfamily of short D-xylulokinases and RbtK (D-ribulokinase; 535 aa) to the subfamily of long kinases. The repressor, dehydrogenase and kinase genes did not show extensive similarity beyond local motifs. This contrasts with the ion symporters (86.6% identity) and their genes (82.7% identity). Due to their unusually high similarity, parts of dalT and rbtT have previously been claimed erroneously to correspond to 'inverted repeats' and possible remnants of a 'metabolic transposon' comprising the dal and rbt genes. Other characteristic structures, e.g. a secondary att lambda site and chi-like sites, as well as the conservation of this gene group in E. coli C are also discussed.
authors.affiliation: Universität Osnabrück, Fachbereich Biologie/Chemie, D-49069 Osnabrück, Germany.
authors.forename: H
authors.initials: H
authors.lastname: Heuel
authors.affiliation: Universität Osnabrück, Fachbereich Biologie/Chemie, D-49069 Osnabrück, Germany.
authors.forename: A
authors.initials: A
authors.lastname: Shakeri-Garakani
authors.affiliation: Universität Osnabrück, Fachbereich Biologie/Chemie, D-49069 Osnabrück, Germany.
authors.forename: S
authors.initials: S
authors.lastname: Turgut
authors.affiliation: Universität Osnabrück, Fachbereich Biologie/Chemie, D-49069 Osnabrück, Germany.
authors.forename: J W
authors.initials: JW
authors.lastname: Lengeler
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D001483:Base Sequence; D004926:Escherichia coli / Q000235:genetics; D005798:Genes, Bacterial / Q000235:genetics; D007711:Klebsiella pneumoniae / Q000201:enzymology* / Q000235:genetics*; D008969:Molecular Sequence Data; D009876:Operon / Q000235:genetics; D010088:Oxidoreductases / Q000032:analysis / Q000378:metabolism; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000737:chemistry* / Q000235:genetics; D012689:Sequence Homology, Nucleic Acid
chemical_list: D001426:Bacterial Proteins; D010088:Oxidoreductases; C113127:DalK protein, Klebsiella pneumoniae; D017853:Phosphotransferases (Alcohol Group Acceptor); C113128:RbtK protein, Klebsiella pneumoniae