Difference between revisions of "ArgG"

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(Expression and regulation)
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= Categories containing this gene/protein =
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{{SubtiWiki category|[[biosynthesis/ acquisition of amino acids]]}}
 
=The protein=
 
=The protein=
  

Revision as of 14:58, 30 November 2010

  • Description: argininosuccinate synthase, reversible

Gene name argG
Synonyms
Essential no
Product argininosuccinate synthase, reversible
Function biosynthesis of arginine
Metabolic function and regulation of this protein in SubtiPathways:
Ammonium/ glutamate
MW, pI 44 kDa, 5.028
Gene length, protein length 1209 bp, 403 aa
Immediate neighbours argH, moaB
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
ArgG context.gif
This image was kindly provided by SubtiList







The gene

Basic information

  • Locus tag: BSU29450

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

Categories containing this gene/protein

biosynthesis/ acquisition of amino acids

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)-(L-arginino)succinate (according to Swiss-Prot)
  • Protein family: Type 1 subfamily (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: S-cysteinylation after diamide stress (C187) PubMed
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization: cytoplasm (according to Swiss-Prot)

Database entries

  • Structure: 1KH1 (from Thermus thermophilus, 44% identity, 65% similarity) PubMed
  • KEGG entry: [2]

Additional information

Expression and regulation

  • Regulation:
    • repressed by casamino acids PubMed
    • repressed by arginine (AhrC)
  • Regulatory mechanism:
    • AhrC: transcription repression
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Falko Hochgräfe, Jörg Mostertz, Dierk-Christoph Pöther, Dörte Becher, John D Helmann, Michael Hecker
S-cysteinylation is a general mechanism for thiol protection of Bacillus subtilis proteins after oxidative stress.
J Biol Chem: 2007, 282(36);25981-5
[PubMed:17611193] [WorldCat.org] [DOI] (P p)

Ulrike Mäder, Georg Homuth, Christian Scharf, Knut Büttner, Rüdiger Bode, Michael Hecker
Transcriptome and proteome analysis of Bacillus subtilis gene expression modulated by amino acid availability.
J Bacteriol: 2002, 184(15);4288-95
[PubMed:12107147] [WorldCat.org] [DOI] (P p)