Difference between revisions of "PurF"

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** number of protein molecules per cell (minimal medium with glucose and ammonium): 1094 {{PubMed|24696501}}
 
** number of protein molecules per cell (minimal medium with glucose and ammonium): 1094 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 4774 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 4774 {{PubMed|24696501}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 1287 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 1448 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 2649 {{PubMed|21395229}}
  
 
=Biological materials =
 
=Biological materials =
 
 
* '''Mutant:'''
 
* '''Mutant:'''
  

Revision as of 14:12, 17 April 2014

  • Description: glutamine phosphoribosyldiphosphate amidotransferase

Gene name purF
Synonyms purB
Essential no
Product glutamine phosphoribosyldiphosphate amidotransferase
Function purine biosynthesis
Gene expression levels in SubtiExpress: purF
Metabolic function and regulation of this protein in SubtiPathways:
purF
MW, pI 51 kDa, 5.873
Gene length, protein length 1428 bp, 476 aa
Immediate neighbours purL, purM
Sequences Protein DNA DNA_with_flanks
Genetic context
PurF context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
PurF expression.png




























Categories containing this gene/protein

biosynthesis/ acquisition of nucleotides

This gene is a member of the following regulons

G-box, PurR regulon

The gene

Basic information

  • Locus tag: BSU06490

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: 5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O (according to Swiss-Prot)
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 1GPH, 1AO0 (complex with ADP and GMP)
  • KEGG entry: [3]

Additional information

  • subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

  • Regulation:
    • repressed in the presence of purine nucleotides (PurR) PubMed
    • repressed in the presence of adenine or adenosine(PurR) PubMed
    • repressed in the presence of guanine(G-box) PubMed
  • Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 1094 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 4774 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 1287 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 1448 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 2649 PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References