Abstract. Soil bacteria display their self-defense as an essential disposition to withstand unfavorable rhizobial conditions. They employ those mechanisms through catabolic and/or anabolic metabolisms such as detoxification of xenobiotis or biosynthesis of nutrients de novo. In this study, newly isolated soil bacterium Arthrobacter nicotianae strain PR was identified, characterized and bioinformatically examined to reveal its synthetase gene. The bacterial genomic DNA was probed in PCR with degenerate synthetase primers. The amplified PCR product was cloned and sequenced. The gene and protein sequence analysis was made using MEGA 4 software and BLASTX search of NCBI-linked protein databases. The conserved amino acid residues revealed the match to aldo-keto reductase (AKR). The multiple sequence-data alignments analysis confirmed the AKR, and multiple phylogeneitic data analysis confirmed its relationship with other bacteria. This enzyme, AKR, belongs to a growing oxidoreductase superfamily and metabolizes a wide range of substrates, including aliphatic aldehydes, monosaccharides, steroids, prostaglandins, and xenobiotics. Our phylogenetic study reveals that this protein is potentially vital in assisting bacteria withstand unfavorable soil environmental condition. Since AKR found in many bacteria and eukaryotes like mammals, amphibians etc, the phylogenetic relationship between our soil isolate and other bacteria was significant as it revealed a distant relationship with A. aurescens.
The pyridoxal-5’-phosphate (PLP)-dependent family of enzymes is a very diverse group of proteins that metabolize small molecules like amino acids and sugars, and synthesize cofactors for other metabolic pathways through transamination, decarboxylation, racemization, and substitution reactions. In this study we employed degenerated primer-based PCR amplification, using genomic DNA isolated from the soil bacterium Exiguobacterium acetylicum strain SN as template. We revealed the presence of a PLP-dependent family of enzymes, such as PLP-dependent acyltransferase, and similarity to 8-amino-7-oxononoate synthase. Sequencing analysis and multiple alignment of the thymidine-adenine-cloned PCR amplicon revealed PLP-dependent family enzymes with specific confering codes and consensus amino acid residues specific to this group of functional proteins. Amino acid residues common to the majority of PLP-dependent enzymes were also revealed by the Lasergene MegAlign software. A phylogenetic tree was constructed. Its analysis revealed a close relationship of E. acetylicum to other bacteria isolated from extreme environments suggesting similarities in anabolic adaptability and evolutionary development.
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