Difference between revisions of "Prs"

From SubtiWiki
Jump to: navigation, search
(Database entries)
(Database entries)
Line 102: Line 102:
 
=== Database entries ===
 
=== Database entries ===
  
* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1IBS 1IBS] [http://www.rcsb.org/pdb/explore.do?structureId=1DKR 1DKR]
+
* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1IBS 1IBS] [http://www.rcsb.org/pdb/explore.do?structureId=1DKR 1DKR][http://www.rcsb.org/pdb/explore.do?structureId=1DKU 1DKU]
  
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P14193 P14193]
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P14193 P14193]

Revision as of 08:31, 10 July 2013

Gene name prs
Synonyms
Essential yes PubMed
Product phosphoribosylpyrophosphate synthetase
Function phosphoribosylpyrophosphate synthesis
(biosynthesis of histidine)
Gene expression levels in SubtiExpress: prs
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
Sequences Protein DNA DNA_with_flanks
Genetic context
Prs context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Prs expression.png




























Categories containing this gene/protein

biosynthesis/ acquisition of amino acids, biosynthesis/ acquisition of nucleotides, 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.: 2008, 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)