Bioinformatic analysis for structure and function of Glutamine synthetase(GS)

TL;DR

This study used bioinformatics tools to predict the structure and function of Glutamine synthetase from Pseudoalteromonas sp., providing insights into its biological role and evolutionary relationships.

Contribution

The paper presents a comprehensive bioinformatics analysis of GS from Pseudoalteromonas sp., including structural and functional predictions, which is novel for this specific organism.

Findings

GS consists of 468 amino acids with a molecular weight of ~52 kDa.

The protein is evolutionarily close to Shewanella oneidensis.

GS lacks signal peptides and transmembrane domains.

Abstract

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.