Difference between revisions of "GlnA"

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* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P12425 P12425]
 
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P12425 P12425]
  
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU17460]
+
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU17460 BSU17460]
  
 
* '''E.C. number:''' [http://www.expasy.org/enzyme/6.3.1.2 6.3.1.2]  
 
* '''E.C. number:''' [http://www.expasy.org/enzyme/6.3.1.2 6.3.1.2]  

Revision as of 22:59, 13 May 2009

  • Description: glutamine synthetase

Gene name glnA
Synonyms
Essential no
Product trigger enzyme: glutamine synthetase
Function glutamine biosynthesis, control of TnrA and GlnR activity
MW, pI 50 kDa, 4.874
Gene length, protein length 1332 bp, 444 aa
Immediate neighbours glnR, ynxB
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
GlnA context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Coordinates:

Phenotypes of a mutant

auxotrophic for glutamine

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information: K(M) for: Glu: 27 mM, ATP: 2.4 mM, ammonium: 0.18 mM; v(max): 3.7 µmol/min/mg
  • Domains: glutamate binding flap (aa 300 ... 306: protects unstable intermediates from abberant hydrolysis)
  • Modification: phosphorylated on ser/ thr/ tyr PubMed
  • Cofactor(s): Mg(2+)
  • Effectors of protein activity: feedback inhibition by glutamine, glutamine binds thhe entrance site for glutamate
  • Localization: cytoplasm (according to Swiss-Prot)

Database entries

  • Structure:


Additional information

GlnA is a homooligomer of 12 subunits

Expression and regulation

  • Regulation: expressed in the absence of glutamine PubMed
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:

Labs working on this gene/protein

Susan Fisher, Boston, USA homepage

Your additional remarks

References

  1. Lévine et al. (2006) Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes. Proteomics 6: 2157-2173 PubMed
  2. Brown, S. W., and A. L. Sonenshein. 1996. Autogenous regulation of the Bacillus subtilis glnRA operon. J. Bacteriol. 178: 2450-2454. PubMed
  3. Wray LV Jr, Zalieckas JM, Fisher SH. (2001) Bacillus subtilis glutamine synthetase controls gene expression through protein-protein interaction with transcription factor TnrA. Cell 107:427-435. PubMed
  4. Fisher, S. H., and Wray, L. V., Jr. (2006) Feedback-resistant mutations in Bacillus subtilis glutamine synthetase are clustered in the active site. J Bacteriol 188: 5966-5974. PubMed
  5. Fisher SH, Sonenshein AL (1984) Bacillus subtilis glutamine synthetase mutants pleiotropically altered in catabolite repression. J Bacteriol 157:612-621. PubMed
  6. Fisher, S. H., Brandenburg, J. L. & Wray, L. V. (2002). Mutations in Bacillus subtilis glutamine synthetase that block its interaction with transcription factor TnrA. Mol Microbiol 45, 627-635. PubMed
  7. Schreier, H. J., Brown, S. W., Hirschi, K. D., Nomellini, J. F. & Sonenshein, A. L. (1989). Regulation of Bacillus subtilis glutamine synthetase gene expression by the product of the glnR gene. J Mol Biol 210, 51-63. PubMed
  8. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed