Abstract: In order to further analyze the structure and bioinformatics function of glutamate racemase, the experiment used γ-PGA-producing strain Bacillus licheniformis DY136 as the material; the glutamic acid racemase gene racE was amplified by PCR, the target gene was purified for prokaryotic expression, and a variety of online bioinformatics analysis softwares were used to analyze its physicochemical properties, hydrophilicity/hydrophobicity, signal peptide, structural domain, etc. The results showed that the size of the PCR-amplified racE gene was 819 bp. Prokaryotic expression of the racE gene was carried out in E. coli; by constructing an expression vector and optimizing expression conditions, a recombinant fusion protein with a size of 30.15 ku was successfully expressed. racE protein encoding 272 amino acids. The amino acid sequence was 99.62% homologous to the Bacillus licheniformis racE protein published in NCBI（GenBank registration number KAA0845975.1）. racE protein was stable in physicochemical properties, which was a hydrophilic protein without transmembrane domain and signal peptide. α-helix was its main secondary structure, which was mainly located in the cytoplasm（73.90%）. The results suggested that the racE gene was conserved and relatively stable, and played an important role in the synthesis of glutamate.