GltA

From SubtiWiki
Revision as of 08:12, 24 September 2014 by Jstuelk (talk | contribs) (Biological materials)
Jump to: navigation, search
  • Description: large subunit of glutamate synthase

Gene name gltA
Synonyms
Essential no
Product glutamate synthase (large subunit)
Function glutamate biosynthesis
Gene expression levels in SubtiExpress: gltA
Interactions involving this protein in SubtInteract: GltA
Metabolic function and regulation of this protein in SubtiPathways:
gltA
MW, pI 168 kDa, 5.47
Gene length, protein length 4560 bp, 1520 amino acids
Immediate neighbours gltB, gltC
Sequences Protein DNA DNA_with_flanks
Genetic context
GltA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
GltA expression.png
















Categories containing this gene/protein

biosynthesis/ acquisition of amino acids, glutamate metabolism, membrane proteins, phosphoproteins

This gene is a member of the following regulons

GltC regulon, FsrA regulon, TnrA regulon, Efp-dependent proteins

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:
    • phosphorylated on Arg-904 AND/OR Arg-914 PubMed
  • Cofactor(s): 3Fe-4S, FAD, FMN
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]

Additional information

  • subject to Clp-dependent proteolysis upon glucose starvation PubMed
  • translation is likely to require Efp due to the presence of several consecutive proline residues PubMed

Expression and regulation

  • Regulation:
    • expression activated by glucose (11 fold) (CcpA, GltC) PubMed
    • repressed by arginine (GltC, RocG) PubMed
    • expressed in the presence of ammonium PubMed
    • repressed in the absence of good nitrogen sources (glutamine or ammonium) (TnrA) PubMed
    • part of the iron sparing response, strong down-regulation in a fur mutant (Fur, FsrA) PubMed
  • Additional information:
    • subject to Clp-dependent proteolysis upon glucose starvation PubMed
    • translation is likely to require Efp due to the presence of several consecutive proline residues PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 2409 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 609 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 285 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 104 PubMed

Biological materials

  • Expression vector:
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab
  • Antibody:

Labs working on this gene/protein

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

Jörg Stülke, University of Göttingen, Germany Homepage

Fabian Commichau University of Göttingen, Germany Homepage

Your additional remarks

References

Reviews


Original publications