Difference between revisions of "GltA"

From SubtiWiki
Jump to: navigation, search
Line 148: Line 148:
 
** subject to Clp-dependent proteolysis upon glucose starvation {{PubMed|17981983}}
 
** subject to Clp-dependent proteolysis upon glucose starvation {{PubMed|17981983}}
 
** [[translation]] is likely to require [[Efp]] due to the presence of several consecutive proline residues {{PubMed|23239624,23239623}}
 
** [[translation]] is likely to require [[Efp]] due to the presence of several consecutive proline residues {{PubMed|23239624,23239623}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium): 2409 {{PubMed|24696501}}
  
 
=Biological materials =
 
=Biological materials =

Revision as of 09:58, 17 April 2014

  • 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

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

Fabian Commichau University of Göttingen, Germany Homepage

Your additional remarks

References

Reviews

Katrin Gunka, Fabian M Commichau
Control of glutamate homeostasis in Bacillus subtilis: a complex interplay between ammonium assimilation, glutamate biosynthesis and degradation.
Mol Microbiol: 2012, 85(2);213-24
[PubMed:22625175] [WorldCat.org] [DOI] (I p)

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