N link to NCBI taxonomic web page and E link to ESTHER gene locus found in this strain. > cellular organisms: NE > Bacteria: NE > Proteobacteria: NE > Gammaproteobacteria: NE > Pseudomonadales: NE > Moraxellaceae: NE > Moraxella: NE > Moraxella sp.: NE
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acide identity. You can retrieve all strain data
N link to NCBI taxonomic web page and E link to ESTHER gene locus found in this strain. Comamonas acidovorans: N, E.
Delftia acidovorans: N, E.
Delftia acidovorans SPH-1: N, E.
Delftia acidovorans CCUG 15835: N, E.
Delftia acidovorans CCUG 274B: N, E.
Moraxella sp. B: N, E.
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MDFPGFKNSTVTVDGVDIAYTVSGEGPPVLMLHGFPQNRAMWARVAPQLA EHHTVVCADLRGYGDSDKPKCLPDRSNYSFRTFAHDQLCVMRHLGFERFH LVGHDRGGRTGHRMALDHPEAVLSLTVMDIVPTYAMFMNTNRLVAASYWH WYFLQQPEPFPEHMIGQDPDFFYETCLFGWGATKVSDFDQQMLNAYRESW RNPAMIHGSCSDYRAAATIDLEHDSADIQRKVECPTLVFYGSKGQMGQLF DIPAEWAKRCNNTTNASLPGGHFFVDQFPAETSEILLKFLARNG
Title: Structure of haloacetate-catabolic IncP-1beta plasmid pUO1 and genetic mobility of its residing haloacetate-catabolic transposon Sota M, Kawasaki H, Tsuda M Ref: Journal of Bacteriology, 185:6741, 2003 : PubMed
The self-transmissible plasmid pUO1 from Delftia acidovorans strain B carries two haloacetate-catabolic transposons, TnHad1 and TnHad2, and the mer genes for resistance to mercury. The complete 67,066-bp sequence of pUO1 revealed that the mer genes were also carried by two Tn402/Tn5053-like transposons, Tn4671 and Tn4672, and that the pUO1 backbone regions shared 99% identity to those of the archetype IncP-1beta plasmid R751. Comparison of pUO1 with three other IncP-1beta plasmids illustrated the importance of transposon insertion in the diversity and evolution of this group of plasmids. Mutational analysis of the four outermost residues in the inverted repeats (IRs) of TnHad2, a Tn21-related transposon, revealed a crucial role of the second residue of its IRs in transposition.
Title: Characterization of a class II defective transposon carrying two haloacetate dehalogenase genes from Delftia acidovorans plasmid pUO1 Sota M, Endo M, Nitta K, Kawasaki H, Tsuda M Ref: Applied Environmental Microbiology, 68:2307, 2002 : PubMed
The two haloacetate dehalogenase genes, dehH1 and dehH2, on the 65-kb plasmid pUO1 from Delftia acidovorans strain B were found to be located on transposable elements. The dehH2 gene was carried on an 8.9-kb class I composite transposon (TnHad1) that was flanked by two directly repeated copies of IS1071, IS1071L and IS1071R. The dehH1 gene was also flanked by IS1071L and a truncated version of IS1071 (IS1071N). TnHad1, dehH1, and IS1071N were located on a 15.6-kb class II transposon (TnHad2) whose terminal inverted repeats and res site showed high homology with those of the Tn21-related transposons. TnHad2 was defective in transposition because of its lacking the transposase and resolvase genes. TnHad2 could transpose when the Tn21-encoded transposase and resolvase were supplied in trans. These results demonstrated that Tn Had2 is a defective Tn21-related transposon carrying another class I catabolic transposon.
Title: Lack of homology between two haloacetate dehalogenase genes encoded on a plasmid from Moraxella sp. strain B Kawasaki H, Tsuda K, Matsushita I, Tonomura K Ref: J Gen Microbiol, 138:1317, 1992 : PubMed
Two genes encoding haloacetate dehalogenases, H-1 and H-2, are closely linked on a plasmid from Moraxella sp. strain B. H-1 predominantly acts on fluoroacetate, but H-2 does not. To elucidate the molecular relationship between the two enzymes, we compared their structural genes. Two restriction fragments of the plasmid DNA were subcloned on M13 phages and their nucleotide sequences were determined. The sequence of each fragment contained an open reading frame that was identified as the structural gene for each of the two dehalogenases on the basis of the following criteria; N-terminal amino acid sequence, amino acid composition, and molecular mass. The genes for H-1 and H-2, designated dehH1 and dehH2, respectively, had different sizes (885 bp and 675 bp) and G+C contents (58.3% and 53.4%). Sequence analysis revealed no homology between the two genes. We concluded that the dehalogenases H-1 and H-2 have no enzyme-evolutionary relationship. The deduced amino acid sequence of the dehH1 gene showed significant similarity to those of three hydrolases of Pseudomonas putida and a haloalkane dehalogenase of Xanthobacter autotrophicus. The dehH2 coding region was sandwiched between two repeated sequences about 1.8 kb long, which might play a part in the frequent spontaneous deletion of dehH2 from the plasmid.