Cloning and analysis of pyrG gene encoding orotidine 5-monophosphate decarboxylase of aspergillus oryzae strain S1

Abstract

In this study, the pyrG gene which encodes for orotidine 5-monophosphate decarboxylase (OMP decarboxylase) of Aspergillus oryzae strain S1 was cloned and analysed. This J.8kb A. oryzae pyrG encompasses the 5 '<regulatory flanking region (465 bp), open reading frame (899 bp) and 3 '<regulatory region (475 bp). The pyrG contained one intron a/ position 623-687 bp based on the AUGUSTUS and FGENESH (SoftBerry) analys corresponding to the intron present in the pyrG of A. oryzae (Accession Number: YU811 In silico analysis showed that the enzyme encoded by the A. oryzae S1 pyrG gene has theoretical molecular weight of 30.28 kDa and theoretical pI value of5.92. This enzyme hydrophilic, located in a region outside of the transmembrane and it functions ill I cytoplasm. Five motives such as N-glycosylation site, protein kinase C (PK phosphorylation site, casein kinase II (CK-2) phosphorylation site, N-myristolation SI and orotidine 5-monophoshate decarboxylase active site have been identified in the py amino acid sequence. The three dimensional structure of this enzyme generated via prate homology modeling using the bioinformatic software, Swiss Model, shows that 0 decarboxylase is a protein with an a/jJ barrel structure possessing 8 jJ-strands surroun by 9 a-helices. The amino acid residues involved in the active site have been identified it is located on one of the jJ-strands. The pyrG DNA sequence will be used for complementation of a pyrG auxotroph mutant of A. oryzae