In silico analyses of flavin reductase from citrobacter freundii A1

Abstract

Objective: The aim of the present study was to describe the structural and phylogenetic features of flavin reductase from C.freundii Al using bioinfonnatics tools. Materials and methods:The flavin reductase (Ire) gene from a dye-degrading bacterium, C. freundii Al was isolated and amplified by Polymerase Chain Reaction (peR). The gene encodes for NAD(P)H:flavin oxidoreductase, an enzyme that catalyzes the reduction of soluble flavins by reduced pyridine nucleotides this was believed to be the azoreductase from C. freundii AI. The gene, approximately 0.8 kb was sequenced and in silica analyses of the nucleotide sequence were performed. Results: From phlyogenetic analyses, we observed that flavin reductase enzyme generally existed in most microorganisms and the enzyme from C.freundii Al is conserved among the Gram-negative bacteria. The protein function of the flavin reductase coded was predicted based on the motifs of deduced amino acid sequence. The amino acid sequence of flavin reductase from C. freundii Al was compared with other azoreductases and was found to be a unique NADPH-preferred azoreductase. Conclusion: Hence, in silica characterization of flavin reductase gene presented various features of the gene and this would facilitate molecular studies of the gene and reveal the functional role of the enzyme.