Difference between revisions of "GlnA"

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(Database entries)
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* '''Structure:'''
 
* '''Structure:'''
 
** [http://www.rcsb.org/pdb/explore/explore.do?structureId=3QAJ 3QAJ] (complex with ATP)
 
** [http://www.rcsb.org/pdb/explore/explore.do?structureId=3QAJ 3QAJ] (complex with ATP)
** [http://www.rcsb.org/pdb/101/motm.do?momID=30] (general discussion of GS structure)
+
** [http://www.rcsb.org/pdb/101/motm.do?momID=30 A general discussion of GS structure]
  
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P12425 P12425]
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P12425 P12425]

Revision as of 17:38, 4 May 2012

Gene name glnA
Synonyms
Essential no
Product trigger enzyme: glutamine synthetase
Function glutamine biosynthesis, control of TnrA and GlnR activity
Interactions involving this protein in SubtInteract: GlnA
Metabolic function and regulation of this protein in SubtiPathways:
Ammonium/ glutamate
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
Expression at a glance   PubMed
GlnA expression.png




























Categories containing this gene/protein

biosynthesis/ acquisition of amino acids, transcription factors and their control, trigger enzyme, phosphoproteins

This gene is a member of the following regulons

GlnR regulon, TnrA regulon

The gene

Basic information

  • Locus tag: BSU17460

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: ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine (according to Swiss-Prot)
  • Protein family: glutamine synthetase family (according to Swiss-Prot)
  • 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, in vitro phosphorylated by PrkC on Thr-26, Thr-147, Ser-207, and Thr-286 PubMed
  • Cofactor(s): Mg(2+)
  • Effectors of protein activity: feedback inhibition by glutamine, glutamine binds the entrance site for glutamate

Database entries

  • KEGG entry: [3]

Additional information

GlnA is a homooligomer of 12 subunits

Expression and regulation

  • Regulation:
    • expressed in the absence of glutamine (GlnR) PubMed
    • repressed in the absence of good nitrogen sources (glutamine or ammonium) (TnrA) PubMed
  • Additional information:

Biological materials

  • Mutant: GP247 (cat), available in Stülke lab
  • Expression vector:
    • expression/ purification from E. coli, with N-terminal Strep-tag (in pGP172): pGP174, available in Stülke lab
  • GFP fusion:
  • two-hybrid system:

Labs working on this gene/protein

Susan Fisher, Boston, USA homepage

Your additional remarks

References

Reviews

Fabian M Commichau, Jörg Stülke
Trigger enzymes: bifunctional proteins active in metabolism and in controlling gene expression.
Mol Microbiol: 2008, 67(4);692-702
[PubMed:18086213] [WorldCat.org] [DOI] (P p)

S H Fisher
Regulation of nitrogen metabolism in Bacillus subtilis: vive la différence!
Mol Microbiol: 1999, 32(2);223-32
[PubMed:10231480] [WorldCat.org] [DOI] (P p)

Original publications

Additional publications: PubMed