  Objective: To predict structure and function of Glutamine synthetase (GS)
from Pseudoalteromonas sp. by bioinformatics technology, and to provide a
theoretical basis for further study. Methods: Open reading frame (ORF) of GS
sequence from Pseudoalteromonas sp. was obtained by ORF finder and was
translated into amino acid residue. The structure domain was analyzed by Blast.
By the method of analysis tools: Protparam, ProtScale, SignalP-4.0, TMHMM,
SOPMA, SWISS-MODEL, NCBI SMART-BLAST and MAGA 7.0, the structure and function
of the protein were predicted and analyzed. Results: The results showed that
the sequence was GS with 468 amino acid residues, theoretical molecular weight
was 51986.64 Da. The protein has the closest evolutionary status with
Shewanella oneidensis. Then it had no signal peptide site and transmembrane
domain. Secondary structure of GS contained 35.04% alpha-helix, 16.67% Extended
chain, 5.34% beta-turn, 42.95% RandomCoil. Conclusions: This GU was a variety
of biological functions of protein that may be used as a molecular samples of
microbial nitrogen metabolism in extreme environments.
