Difference between revisions of "Prs"

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m (Reverted edits by 134.76.70.252 (talk) to last revision by Jstuelk)
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* '''Operon:''' ''[[gcaD]]-[[prs]]-[[ctc]]'' [http://www.ncbi.nlm.nih.gov/pubmed/8522540 PubMed]
 
* '''Operon:''' ''[[gcaD]]-[[prs]]-[[ctc]]'' [http://www.ncbi.nlm.nih.gov/pubmed/8522540 PubMed]
  
* '''[[Sigma factor]]:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/pubmed/8522540 PubMed]
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=prs_57745_58698_1 prs] {{PubMed|22383849}}
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* '''Sigma factor:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/pubmed/8522540 PubMed]
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  

Revision as of 10:54, 12 April 2012

Gene name prs
Synonyms
Essential yes PubMed
Product phosphoribosylpyrophosphate synthetase
Function phosphoribosylpyrophosphate synthesis
(biosynthesis of histidine)
Interactions involving this protein in SubtInteract: Prs
Metabolic function and regulation of this protein in SubtiPathways:
Purine synthesis, Nucleotides (regulation), His, Murein recycling
MW, pI 34 kDa, 5.895
Gene length, protein length 951 bp, 317 aa
Immediate neighbours gcaD, ctc
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
Prs context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

biosynthesis/ acquisition of amino acids, essential genes, universally conserved proteins

This gene is a member of the following regulons

stringent response

The gene

Basic information

  • Locus tag: BSU00510

Phenotypes of a mutant

essential PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate (according to Swiss-Prot)
  • Protein family: ribose-phosphate pyrophosphokinase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
    • subject to feedback inhibition by two end products of purine biosynthesis, adenosine 5'-diphosphate (ADP) and guanosine 5'-diphosphate (GDP) PubMed

Database entries

  • KEGG entry: [3]

Additional information

universally conserved protein

Expression and regulation

  • Regulation:
    • RelA dependent downregulation (Class I) during stringent response PubMed
  • Regulatory mechanism:
  • 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

Additional publications: PubMed

Shuobo Shi, Tao Chen, Zhigang Zhang, Xun Chen, Xueming Zhao
Transcriptome analysis guided metabolic engineering of Bacillus subtilis for riboflavin production.
Metab Eng: 2009, 11(4-5);243-52
[PubMed:19446032] [WorldCat.org] [DOI] (I p)

Aloke Kumar Bera, Jianghai Zhu, Howard Zalkin, Janet L Smith
Functional dissection of the Bacillus subtilis pur operator site.
J Bacteriol: 2003, 185(14);4099-109
[PubMed:12837784] [WorldCat.org] [DOI] (P p)

Sangita C Sinha, Joseph Krahn, Byung Sik Shin, Diana R Tomchick, Howard Zalkin, Janet L Smith
The purine repressor of Bacillus subtilis: a novel combination of domains adapted for transcription regulation.
J Bacteriol: 2003, 185(14);4087-98
[PubMed:12837783] [WorldCat.org] [DOI] (P p)

I Hilden, B N Krath, B Hove-Jensen
Tricistronic operon expression of the genes gcaD (tms), which encodes N-acetylglucosamine 1-phosphate uridyltransferase, prs, which encodes phosphoribosyl diphosphate synthetase, and ctc in vegetative cells of Bacillus subtilis.
J Bacteriol: 1995, 177(24);7280-4
[PubMed:8522540] [WorldCat.org] [DOI] (P p)

K Arnvig, B Hove-Jensen, R L Switzer
Purification and properties of phosphoribosyl-diphosphate synthetase from Bacillus subtilis.
Eur J Biochem: 1990, 192(1);195-200
[PubMed:2169413] [WorldCat.org] [DOI] (P p)