Difference between revisions of "PurQ"

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* '''Regulation:'''  
 
* '''Regulation:'''  
 +
** repressed in the presence of purine nucleotides ([[PurR]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/7638212 PubMed]
 
** repressed in the presence of adenine or adenosine([[PurR]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/2536750 PubMed]
 
** repressed in the presence of adenine or adenosine([[PurR]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/2536750 PubMed]
 
** repressed in the presence of guanine([[G-box]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/3036807 PubMed]
 
** repressed in the presence of guanine([[G-box]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/3036807 PubMed]
Line 101: Line 102:
  
 
* '''Regulatory mechanism:'''  
 
* '''Regulatory mechanism:'''  
 +
** [PurR]]: transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/7638212 PubMed]
 
** [[PurR]]: transcription repression (molecular inducer: PRPP) [http://www.ncbi.nlm.nih.gov/sites/entrez/2536750 PubMed]
 
** [[PurR]]: transcription repression (molecular inducer: PRPP) [http://www.ncbi.nlm.nih.gov/sites/entrez/2536750 PubMed]
 
** [[G-box]]: transcription termination/ antitermination ([[riboswitch]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/3036807 PubMed1] [http://www.ncbi.nlm.nih.gov/sites/entrez/12787499 PubMed2]
 
** [[G-box]]: transcription termination/ antitermination ([[riboswitch]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/3036807 PubMed1] [http://www.ncbi.nlm.nih.gov/sites/entrez/12787499 PubMed2]

Revision as of 17:08, 11 June 2009

  • Description: phosphoribosylformylglycinamidine synthase

Gene name purQ
Synonyms
Essential no
Product phosphoribosylformylglycinamidine synthase
Function purine biosynthesis
MW, pI 24 kDa, 4.627
Gene length, protein length 681 bp, 227 aa
Immediate neighbours purS, purL
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
PurQ context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU06470

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H2O = ADP + phosphate + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate (according to Swiss-Prot)
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization: cytoplasm (according to Swiss-Prot)

Database entries

  • Structure:
  • 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
    • expression activated by glucose (4.4 fold) PubMed
  • Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135] [WorldCat.org] [DOI] (P p)

  1. Blencke et al. (2003) Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways. Metab Eng. 5: 133-149 PubMed
  2. Gerth et al. (2008) Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis. J Bacteriol 190:321-331 PubMed
  3. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed