The gdhA gene of B.subtilis natto was cloned into plasmid pET28a and expressed in E.coli BL21 (DE3), and explored the protein structure, structure domains features using bioinformatics methods. This GDH has both NADP+-dependent and NAD+-dependent enzymatic activities, which were 3.140 U/mg protein and 0.251 4 U/mg protein, respectively. The results of informatics analysis showed that the coding region sequence contains a complete ORF (1 275 bp) which encoding 424 amino acids. The molecular weight was 47.05 kDa and theoretical pI was 5.58. The gdhA protein had no transmembrane regions. Its secondary structure was composed of α-helix and random coil. And its tertiary structure showed that the protein formed a dimerization domain and a NAD (P) binding domain in the 45—174 and 191—424 amino acid residues，respectively. The amino acid similarities of dimerization domains and NAD (P) binding domains of B.subtilis natto HSF 1410 and E.coli gdhA protein were 29.23% and 29.27%，respectively. These were significantly higher than gdhA amino acids of B.subtilis 168. Compared to B.subtilis 168 gdhA，B.subtilis natto HSF 1410 and E.coli gdhA are more similar in the space structure，the bacteria is mainly responsible for promoting α- ketone glutaric acid into glutamic acid.

Bacillus subtilis natto HSF 1410; GDH; cDNA; cloning; bioinformatics analysis