Difference between revisions of "GltA"

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(Categories containing this gene/protein)
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= [[Categories]] containing this gene/protein =
 
= [[Categories]] containing this gene/protein =
 
{{SubtiWiki category|[[biosynthesis/ acquisition of amino acids]]}},
 
{{SubtiWiki category|[[biosynthesis/ acquisition of amino acids]]}},
{{SubtiWiki category|[[membrane proteins]]}}
+
{{SubtiWiki category|[[membrane proteins]]}},
 +
{{SubtiWiki category|[[phosphoproteins]]}}
  
 
= This gene is a member of the following [[regulons]] =
 
= This gene is a member of the following [[regulons]] =

Revision as of 15:19, 20 April 2012

  • Description: large subunit of glutamate synthase

Gene name gltA
Synonyms
Essential no
Product glutamate synthase (large subunit)
Function glutamate biosynthesis
Interactions involving this protein in SubtInteract: GltA
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 gltB, gltC
Get the DNA and protein sequences
(Barbe et al., 2009)
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, membrane proteins, phosphoproteins

This gene is a member of the following regulons

GltC regulon, FsrA regulon, TnrA regulon

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:

Database entries

  • KEGG entry: [3]

Additional information

subject to Clp-dependent proteolysis upon glucose starvation 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

Biological materials

  • Mutant: GP807 (del gltAB::tet), GP222 (gltA under the control of p-xyl), available in Stülke lab
  • Expression vector:
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
  • 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

Reviews

Akira Suzuki, David B Knaff
Glutamate synthase: structural, mechanistic and regulatory properties, and role in the amino acid metabolism.
Photosynth Res: 2005, 83(2);191-217
[PubMed:16143852] [WorldCat.org] [DOI] (P p)

Frank M Raushel, James B Thoden, Hazel M Holden
Enzymes with molecular tunnels.
Acc Chem Res: 2003, 36(7);539-48
[PubMed:12859215] [WorldCat.org] [DOI] (P p)

Original publications