Homology study of two polyhydroxyalkanoate (PHA) synthases from Pseudomonas aureofaciens.
Recently, we have cloned and analyzed two polyhydroxyalkanoate (PHA) synthase genes (phaC1 and phaC2 in the pha cluster) from Pseudomonas aureofaciens. In this report, the deduced amino acid (AA) sequences of PHA synthase 1 and PHA synthase 2 from P. aureofaciens are compared with those from three other bacterial strains (Pseudomonas sp. 61-3, P. oleovorans and P. aeruginosa) containing the homologous pha cluster. The level of homology of either PHA synthase 1 or PHA synthase 2 was high with each enzyme from these three bacterial strains. Furthermore, multialignment of PHA synthase AA sequences implied that both enzymes of PHA synthase 1 and PHA synthase 2 were highly conserved in the four strains including P. aureofaciens.
Umeda
F
F
Graduate School of Pharmaceutical Sciences, Osaka University, Suita, Japan.
Nishikawa
T
T
Miyasaka
H
H
Maeda
I
I
Kawase
M
M
Yagi
K
K
D000217:Acyltransferases / Q000235:genetics*; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics*; D007527:Isoenzymes / Q000235:genetics; D008969:Molecular Sequence Data; D011549:Pseudomonas / Q000235:genetics*; D016415:Sequence Alignment; D017385:Sequence Homology
D001426:Bacterial Proteins; D007527:Isoenzymes; D000217:Acyltransferases; C077225:poly(3-hydroxyalkanoic acid) synthase