• Microbiology and Biotechnology Letters
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• v.25 no.4
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• pp.367-373
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• 1997

One of the three components of the phenanthrene dioxygenase which is required for conversion of phenanthrene to cis-phenanthrene dihydrodiol, Rieske-type ferredoxin encoded by phnR has been cloned and sequenced from Pseudomonas sp. strain DJ77. The gene phnR is positioned at the downstream of phnQ encoding 2,3-dihydroxybiphenyl 1,2-dioxygenase. The PhnR ferredoxin contains 108 amino acids with a Mr of 11,355. The deduced amino acid sequence of the PhnR ferredoxin is 35-79% identical to those of homologous ferredoxins encoded by various genes.

• Korean Journal of Microbiology
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• v.30 no.1
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• pp.1-7
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• 1992

We cloned a gene cluster encoding phenanthrene-degrading enzymes on a 6.8-kb Xhol fragment from the Pseudomonas sp. DJ77 chromosomal DNA into the vector pBLUESCRIPT SIC(+). The resultant clone, containing the recombinant plilsmid pHENX7, was able to convert 3-methylcatechol to a yellow mela-cleavage compound. Since the pHENX7R in which the DNA insert was cloned in the opposite orientation lacked extradiol dioxygenase activity. the direction of transcription was established. Four polypeptides, PhnC (24 kDa). PhnD (31 kDa), PhnE (34 kDa). and PhnF (15 kDa), were identified in E coli JM101 transformed with several pHENX7-derived plasmids. The locations and extents of ~ndividual genes were determined by subcloning. The gene order was phnC-phnD-phnE-phnF-phnG, and phnC, phnD, phnE, and phnG genes encoded glutathione S-transferase, mrta-cleavage compound hydrolase, extradiol dioxygenase, mera-cleavage compound dehydrogenase, respectively.

• Korean Journal of Microbiology
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• v.39 no.3
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• pp.123-127
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• 2003

Sphingomonas chungbukensis DJ77 is able to metabolize phenanthrene as the sole carbon and energy source. The plasmid pUPX5 includes phnS gene encoding 2-hydroxychromene-2-carboxylate (HCCA) isomerase, which is needed for phenanthrene and naphthanene degradation. We determined the nucleotide sequence of DNA fragment of 3271 bp which included the phnS gene. The fragment included an open reading frame of 594 bp which has ATG initiation codon and TAA termination codon and GGAA ribosomal binding site. The predicted amino acid sequence of the enzyme consists of 198 amino acids. The deduced amino acid sequence of the phnS enzyme exhibited 94％ identity with that of the corresponding enzyme in Sphingomonas aromaticivorans F199. The phnS gene is located downstream and in the same operon as phnQ and phnR, encoding a 2,3-dihydroxybiphenyl 1,2-dioxygenase and a ferredoxin component of biphenyl dioxygenase, respectively.

• Korean Journal of Microbiology
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• v.34 no.3
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• pp.115-119
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• 1998

We cloned the 4.8 kb BglII fragment containing genes downstream pHENX7 from Pseudomonas sp. strain DJ77. The restriction map of the resultant clone, recombinant plasmid pYCS500, was determined. Sequencing analysis of the 465 bp HindIII-ClaI fragment revealed an open reading frame of 282 bp that was then designated phnM. The deduced polypeptide is 93 amino acid residues long with a $M_r$ of 10,008. The PhnM has 37.3-53.9% identity with plant-type ferredoxin proteins such as NahT, XylT, DmpQ, AtdS, PhlG, PhhQ and TbuW and contains the motif similar to well-conserved functional domains of those proteins.