Difference between revisions of "PupG"

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= This gene is a member of the following [[regulons]] =
 
= This gene is a member of the following [[regulons]] =
 
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{{SubtiWiki regulon|[[CcpA regulon]]}}
  
 
=The gene=
 
=The gene=
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=== Additional information===
 
=== Additional information===
 
 
  
  
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* '''Regulation:'''  
 
* '''Regulation:'''  
 
** induced in the presence of nucleosides (deoxyribose 5-phosphate and ribose 5-phosphate act as molecular inducers) {{PubMed|10537218}}  
 
** induced in the presence of nucleosides (deoxyribose 5-phosphate and ribose 5-phosphate act as molecular inducers) {{PubMed|10537218}}  
** subject to repression by glucose {{PubMed|10537218}}  
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** subject to carbon catabolite repression ([[CcpA]]) {{PubMed|22900538,10537218}}
  
 
* '''Regulatory mechanism:'''  
 
* '''Regulatory mechanism:'''  
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** [[CcpA]]:  transcription repression {{PubMed|22900538}}
  
 
* '''Additional information:'''
 
* '''Additional information:'''
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=References=
 
=References=
  
<pubmed>10537218,,17218307, </pubmed>
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<pubmed>10537218,22900538,17218307, </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 16:33, 21 August 2012

  • Description: purine nucleoside phosphorylase

Gene name pupG
Synonyms punA, pnp, yqkO
Essential no
Product purine nucleoside phosphorylase
Function purine salvage and interconversion
Gene expression levels in SubtiExpress: pupG
Metabolic function and regulation of this protein in SubtiPathways:
Purine salvage, Nucleoside catabolism, Nucleotides (regulation)
MW, pI 28 kDa, 4.86
Gene length, protein length 813 bp, 271 aa
Immediate neighbours dacF, drm
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
PunA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
PupG expression.png



















Categories containing this gene/protein

biosynthesis/ acquisition of nucleotides, phosphoproteins

This gene is a member of the following regulons

CcpA regulon

The gene

Basic information

  • Locus tag: BSU23490

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate (according to Swiss-Prot) RNA(n+1) + phosphate = RNA(n) + a nucleoside diphosphate (according to Swiss-Prot)
  • Protein family: PNP/MTAP phosphorylase family (according to Swiss-Prot) polyribonucleotide nucleotidyltransferase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: phosphorylation on Ser-28 PubMed
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • induced in the presence of nucleosides (deoxyribose 5-phosphate and ribose 5-phosphate act as molecular inducers) PubMed
    • subject to carbon catabolite repression (CcpA) 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

Bogumiła C Marciniak, Monika Pabijaniak, Anne de Jong, Robert Dűhring, Gerald Seidel, Wolfgang Hillen, Oscar P Kuipers
High- and low-affinity cre boxes for CcpA binding in Bacillus subtilis revealed by genome-wide analysis.
BMC Genomics: 2012, 13;401
[PubMed:22900538] [WorldCat.org] [DOI] (I e)

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [WorldCat.org] [DOI] (P p)

R Schuch, A Garibian, H H Saxild, P J Piggot, P Nygaard
Nucleosides as a carbon source in Bacillus subtilis: characterization of the drm-pupG operon.
Microbiology (Reading): 1999, 145 ( Pt 10);2957-66
[PubMed:10537218] [WorldCat.org] [DOI] (P p)