Difference between revisions of "ArgC"

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* '''Additional information:'''
 
* '''Additional information:'''
 
** number of protein molecules per cell (minimal medium with glucose and ammonium): 419 {{PubMed|24696501}}
 
** number of protein molecules per cell (minimal medium with glucose and ammonium): 419 {{PubMed|24696501}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 389 {{PubMed|21395229}}
 +
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 772 {{PubMed|21395229}}
  
 
=Biological materials =
 
=Biological materials =
 
 
* '''Mutant:'''
 
* '''Mutant:'''
  

Revision as of 13:32, 17 April 2014

  • Description: N-acetyl-g-glutamyl-phosphate reductase

Gene name argC
Synonyms
Essential no
Product N-acetyl-g-glutamyl-phosphate reductase
Function biosynthesis of arginine
Gene expression levels in SubtiExpress: argC
Metabolic function and regulation of this protein in SubtiPathways:
argC
MW, pI 37 kDa, 5.167
Gene length, protein length 1038 bp, 346 aa
Immediate neighbours yitZ, argJ
Sequences Protein DNA DNA_with_flanks
Genetic context
ArgC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
ArgC expression.png




























Categories containing this gene/protein

biosynthesis/ acquisition of amino acids

This gene is a member of the following regulons

AhrC regulon

The gene

Basic information

  • Locus tag: BSU11190

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate = N-acetyl-5-glutamyl phosphate + NADPH (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:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 419 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 389 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 772 PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

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)

M O'Reilly, K Woodson, B C Dowds, K M Devine
The citrulline biosynthetic operon, argC-F, and a ribose transport operon, rbs, from Bacillus subtilis are negatively regulated by Spo0A.
Mol Microbiol: 1994, 11(1);87-98
[PubMed:7511775] [WorldCat.org] [DOI] (P p)

M C Smith, A Mountain, S Baumberg
Nucleotide sequence of the Bacillus subtilis argC gene encoding N-acetylglutamate-gamma-semialdehyde dehydrogenase.
Nucleic Acids Res: 1990, 18(15);4595
[PubMed:2117746] [WorldCat.org] [DOI] (P p)

A Mountain, N H Mann, R N Munton, S Baumberg
Cloning of a Bacillus subtilis restriction fragment complementing auxotrophic mutants of eight Escherichia coli genes of arginine biosynthesis.
Mol Gen Genet: 1984, 197(1);82-9
[PubMed:6096675] [WorldCat.org] [DOI] (P p)