Difference between revisions of "GltB"

From SubtiWiki
Jump to: navigation, search
(References)
Line 85: Line 85:
 
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/O34399]
 
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/O34399]
  
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU18440]
+
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU18440]
  
 
* '''E.C. number:''' [http://www.expasy.ch/cgi-bin/get-enzyme-entry?1.4.1.13]
 
* '''E.C. number:''' [http://www.expasy.ch/cgi-bin/get-enzyme-entry?1.4.1.13]

Revision as of 16:51, 19 March 2009

  • Description: small subunit of glutamate synthase

Gene name gltB
Synonyms
Essential no
Product glutamate synthase (small subunit)
Function glutamate biosynthesis
MW, pI 54.6 kDa, 7.69
Gene length, protein length 1479 bp, 493 amino acids
Immediate neighbours gltA, yogA
Gene sequence (+200bp) corrected Protein sequence
Caution: The sequence for this gene in SubtiList contains errors
Genetic context
GltB context.gif




The gene

Basic information

  • Coordinates: 2007785 - 2009263

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
  • Protein family: glutamate synthase family.
  • Paralogous protein(s): none

Extended information on the protein

  • Kinetic information:
  • Domains:
    • nucleotide binding domain (NADP) (299–313)
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization:

Database entries

  • Structure:
  • Swiss prot entry: [3]
  • KEGG entry: [4]
  • E.C. number: [5]

Additional information

Expression and regulation

  • Regulation: see gltA
  • Additional information:

Biological materials

  • Mutant: GP807 (del gltAB::tet), GP736 (spc), available in Stülke lab
  • Expression vector: pGP1119 (in pGP380, for SPINE, expression in B. subtilis), available in Stülke lab
  • lacZ fusion: see gltA
  • 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

  1. Yoshida K, et al. (2003) Identification of additional TnrA-regulated genes of Bacillus subtilis associated with a TnrA box. Mol Microbiol 49(1): 157-65. PubMed
  2. Belitsky, B. R., and Sonenshein, A. L. (1995) Mutations in GltC that increase Bacillus subtilis gltA expression. J Bacteriol 177: 5696-5700.PubMed
  3. Belitsky, B. R., and Sonenshein, A. L. (2004) Modulation of activity of Bacillus subtilis regulatory proteins GltC and TnrA by glutamate dehydrogenase. J Bacteriol 186: 3399-3407.PubMed
  4. Bohannon, D. E., and Sonenshein, A. L. (1989) Positive regulation of glutamate biosynthesis in Bacillus subtilis. J Bacteriol 171: 4718-4727.PubMed
  5. Commichau, F. M., Wacker, I., Schleider, J., Blencke, H.-M., Reif, I., Tripal, P., and Stülke, J. (2007) Characterization of Bacillus subtilis mutants with carbon source-independent glutamate biosynthesis. J Mol Microbiol Biotechnol 12: 106-113. PubMed
  6. Commichau, F. M., Herzberg, C., Tripal, P., Valerius, O., and Stülke, J. (2007) A regulatory protein-protein interaction governs glutamate biosynthesis in Bacillus subtilis: The glutamate dehydrogenase RocG moonlights in controlling the transcription factor GltC. Mol Microbiol 65: 642-654. PubMed
  7. Picossi, S., Belitsky, B. R., and Sonenshein, A. L. (2007) Molecular mechanism of the regulation of Bacillus subtilis gltAB expression by GltC. J Mol Biol 365: 1298-1313. PubMed
  8. Wacker, I., Ludwig, H., Reif, I., Blencke, H. M., Detsch, C., and Stülke, J. (2003) The regulatory link between carbon and nitrogen metabolism in Bacillus subtilis: regulation of the gltAB operon by the catabolite control protein CcpA. Microbiology 149: 3001-3009.PubMed
  9. Belitsky, B. R., Wray, L. V., Jr., Fisher, S. H., Bohannon, D. E. & Sonenshein, A. L. (2000). Role of TnrA in nitrogen source-dependent repression of Bacillus subtilis glutamate synthase gene expression. J Bacteriol 182, 5939-5947. PubMed
  10. Commichau, F. M., Gunka, K., Landmann, J. J. & Stülke, J. (2008) Glutamate metabolism in Bacillus subtilis: Gene expression and enzyme activities evolved to avoid futile cycles and to allow rapid responses to perturbations in the system. J. Bacteriol. 190: 3557-3564. PubMed