Abstract: 6-Phogluconate dehydrogenase (6PGDH, EC 1.1.1.44)is one of the key enzymes in the pentose phosphate pathway(PPP). In this study, the 6-phogluconate dehydrogenase gene (gnd) of Aspergillus oryzae CICC2012 was cloned by means of PCR. Subsequently, the bioinformatic methodology was applied to determine the amino acid sequence homology, phylogenetic trees, physical-chemical properties and protein structure of the gene. The results revealed the gene’s length to be 1 723 bp, which encompassed an open reading frame with 1 551 bp encoding 516 amino acids. The 6PGDH encoded by gnd showed a 99% homology with the 6PGDH gene of Aspergillus flavus, which had 11 serine phosphorylation sites, 2 threonine phosphorylation sites and 6 tyrosine phosphorylation sites. The 6PGDH had a molecular weight of 57.3 kD and an isoelectric point of 5.63. The secondary structure of the gnd protein was 44.57% alpha helix, 12.79% beta sheet and 42.64% random coil. The 11-195 amino acid residues appeared to be the NADP+ binding sites.