Difference between revisions of "GltA"

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<pubmed>12823818,,11029411,12850135 7559360 15150225 2548995 17183217, 17608797,17134717,14523131,12823818, 18326565,17981983,18763711  </pubmed>
 
<pubmed>12823818,,11029411,12850135 7559360 15150225 2548995 17183217, 17608797,17134717,14523131,12823818, 18326565,17981983,18763711  </pubmed>
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[[Category:Protein-coding genes]]

Revision as of 11:04, 21 July 2009

  • Description: large subunit of glutamate synthase

Gene name gltA
Synonyms
Essential no
Product glutamate synthase (large subunit)
Function glutamate biosynthesis
Metabolic function and regulation of this protein in SubtiPathways:
Ammonium/ glutamate
MW, pI 168 kDa, 5.47
Gene length, protein length 4560 bp, 1520 amino acids
Immediate neighbours gltC, gltB
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
GltA context.gif
This image was kindly provided by SubtiList








The gene

Basic information

  • Locus tag: BSU18450

Phenotypes of a mutant

auxotrophic for glutamate

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: 2 L-glutamate + NADP+ = L-glutamine + 2-oxoglutarate + NADPH (according to Swiss-Prot) 2 L-glutamate + NADP(+) <=> L-glutamine + 2-oxoglutarate + NADPH
  • Protein family: glutamate synthase family (according to Swiss-Prot) glutamate synthase family
  • Paralogous protein(s): YerD

Extended information on the protein

  • Kinetic information:
  • Domains:
    • Glutamine amidotransferase type-2 domain (22-415)
    • Nucleotide binding domain (1060-1112)
  • Modification:
  • Cofactor(s): 3Fe-4S, FAD, FMN
  • Effectors of protein activity:
  • Interactions:
  • Localization: membrane associated PubMed, cytoplasm

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

  • Regulation: expression activated by glucose (11 fold) PubMed, induced by sugar PubMed, repressed by arginine PubMed, ammonium required PubMed
    • repressed in the absence of good nitrogen sources (glutamine or ammonium) (TnrA) PubMed
  • Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed

Biological materials

  • Mutant: GP807 (del gltAB::tet), GP222 (gltA under the control of p-xyl), available in Stülke lab
  • Expression vector:
  • GFP fusion:
  • Antibody:

Labs working on this gene/protein

Linc Sonenshein, Tufts University, Boston, MA, USA Homepage

Jörg Stülke, University of Göttingen, Germany Homepage

Your additional remarks

References