Glutamate dehydrogenase (GDH) is found widely in many plants, animals and microorganisms as a mitochondrial enzyme, and it is the key enzyme in amino acid catabolism. It is distributed extensively in animal tissues such as the hepatopancreas, kidney and brain. GDH activity is very strong and it may catalyze the glutamic acid oxidative deamination reaction. To explore the function of the GDH gene during ammonia nitrogen metabolism of black tiger shrimps ( (denoted ) was obtained by rapid amplification of cDNA ends. The full length of the sequence of was 2386 bp containing a 5'UTR of 21 bp and a 3'UTR of 688 bp, and the length of the open reading frame (ORF) was 1677 bp encoding 558 amino acids. The predicted molecular mass of the amino acid (aa) sequence was 61.837 kD with an estimated pI of 6.57, and there was a poly A with 27 bp. In common with the GDH of other animals, the structure of the protein contained two conservative domains, ELFV dehydrog N and NAD bind 1 Glu DH. There were 37 phosphorylation sites and three glycosylation sites in this protein. Through multiple sequence alignment and phylogenetic tree analysis, it was concluded that the homology and similarity between was the highest. Analysis of the tissue expression pattern of mRNA was expressed in all tissues tested, including lymphoid tissue, ovary, eyestalk nerve, brain, stomach, muscle, intestines, thoracic nerve, hemolymph, hepatopancreas and gill. The highest levels were found in muscle, the next highest in the eyestalk and the lowest levels in the hemolymph. To study the functions of under conditions of ammonia nitrogen stress, the hepatopancreas and gill were sampled at 6 h, 12 h, 24 h, 48 h, 72 h and 96 h after exposure to different concentrations of ammonia nitrogen. The expression of in the hepatopancreas and gill was significantly different compared with the control group (<0.05), and the expression levels differed between hepatopancreas and gill. The results showed that may play an important role in shrimp ammonia metabolism and may be involved in responses to acute ammonia stress.