Difference between revisions of "Sandbox"

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* '''Description:''' Enzyme I, general (non sugar-specific) component of the PTS. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein ([[PtsH |HPr]])  <br/><br/>
+
* '''Description:''' purine nucleoside phosphorylase <br/><br/>
  
 
{| align="right" border="1" cellpadding="2"  
 
{| align="right" border="1" cellpadding="2"  
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"|'''Gene name'''
 
|style="background:#ABCDEF;" align="center"|'''Gene name'''
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|''ptsI''
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|''punA''
 
|-
 
|-
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|style="background:#ABCDEF;" align="center"| '''Synonyms''' || '' ''
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|style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''pnp, yqkO ''
 
|-
 
|-
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|style="background:#ABCDEF;" align="center"| '''Essential''' || no
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|style="background:#ABCDEF;" align="center"| '''Essential''' || no  
 
|-
 
|-
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|style="background:#ABCDEF;" align="center"| '''Product''' || phosphotransferase system (PTS) enzyme I
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|style="background:#ABCDEF;" align="center"| '''Product''' || purine nucleoside phosphorylase
 
|-
 
|-
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|style="background:#ABCDEF;" align="center"|'''Function''' || PTS-dependent sugar transport
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|style="background:#ABCDEF;" align="center"|'''Function''' || purine salvage and interconversion
 
|-
 
|-
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|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 62,9 kDa, 4.59
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|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 28 kDa, 4.86 
 
|-
 
|-
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|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1710 bp, 570 amino acids
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|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 813 bp, 271 aa
 
|-
 
|-
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ptsH]]'', ''[[splA]]''
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[dacF]]'', ''[[drm]]''
 
|-
 
|-
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|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB13264&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
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|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB14281&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
 
|-
 
|-
−
|-
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|colspan="2" | '''Genetic context''' <br/> [[Image:punA_context.gif]]
−
|-
 
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|colspan="2" | '''Genetic context''' <br/> [[Image:ptsI_context.gif]]
 
 
  <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
 
  <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
 
|-
 
|-
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__TOC__
 
__TOC__
  
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<br/><br/><br/><br/>
+
<br/><br/>
  
 
=The gene=
 
=The gene=
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=== Basic information ===
 
=== Basic information ===
  
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* '''Locus tag:''' BSU13910
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* '''Locus tag:''' BSU23490
  
 
===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===
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=== Database entries ===
 
=== Database entries ===
  
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* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/ptsGHI.html]
+
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/drm-punA.html]
  
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* '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG10201]
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* '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG11330]
  
 
=== Additional information===
 
=== Additional information===
 +
  
 
=The protein=
 
=The protein=
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=== Basic information/ Evolution ===
 
=== Basic information/ Evolution ===
  
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* '''Catalyzed reaction/ biological activity:''' Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine (according to Swiss-Prot) PEP-dependent autophosphorylation on His-189, transfer of the phosphoryl group to [[PtsH |HPr]] (His-15)
+
* '''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:''' PEP-utilizing enzyme family (according to Swiss-Prot) PEP-utilizing enzyme family
+
* '''Protein family:''' PNP/MTAP phosphorylase family (according to Swiss-Prot) polyribonucleotide nucleotidyltransferase family (according to Swiss-Prot)
  
 
* '''Paralogous protein(s):'''
 
* '''Paralogous protein(s):'''
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* '''Domains:'''  
 
* '''Domains:'''  
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**HPr binding site (N-Terminal Domain)
 
−
**pyruvate binding site (C-Terminal Domain)
 
−
**pyrophosphate/phosphate carrier histidine (central Domain)
 
  
−
* '''Modification:''' transient autophosphorylation on His-189, in vivo also phosphorylated on Ser-34 or Ser-36 [http://www.ncbi.nlm.nih.gov/pubmed/17218307 PubMed]
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* '''Modification:''' phosphorylation on Ser-28 [http://www.ncbi.nlm.nih.gov/sites/entrez/17218307 PubMed]
  
−
* '''Cofactor(s):''' Magnesium
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* '''Cofactor(s):'''
  
 
* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
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* '''Interactions:'''
 
* '''Interactions:'''
  
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* '''Localization:''' cytoplasm (according to Swiss-Prot),  Cytoplasm
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* '''Localization:''' secreted (according to Swiss-Prot)
  
 
=== Database entries ===
 
=== Database entries ===
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* '''Structure:'''
 
* '''Structure:'''
  
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* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P08838 P08838]
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* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P46354 P46354]
  
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* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU13910]
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* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU23490]
  
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* '''E.C. number:''' [http://www.expasy.org/enzyme/2.7.3.9 2.7.3.9]  2.7.3.9]
+
* '''E.C. number:''' [http://www.expasy.org/enzyme/2.4.2.1 2.4.2.1]  2.7.7.8]
  
 
=== Additional information===
 
=== Additional information===
−
 
  
 
=Expression and regulation=
 
=Expression and regulation=
  
 
* '''Operon:'''  
 
* '''Operon:'''  
−
**''[[ptsG]]-[[ptsH]]-[[ptsI]]''
 
−
**''[[ptsH]]-[[ptsI]]''
 
  
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* '''[[Sigma factor]]:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+11902727 PubMed]
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* '''[[Sigma factor]]:'''  
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* '''Regulation:''' expression activated by glucose (4.3 fold) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed],  induction by glucose (''[[ptsG]]''), constitutive (''[[ptsH]]'')
+
 
 +
* '''Regulation:'''  
  
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* '''Regulatory mechanism:''' ''[[ptsG]]'': transcriptional antitermination via the [[GlcT]]-dependent RNA-switch
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* '''Regulatory mechanism:'''  
  
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* '''Additional information:'''
+
* '''Additional information:'''  
  
 
=Biological materials =
 
=Biological materials =
  
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* '''Mutant:''' GP864 (ermC), available in [[Stülke]] lab
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* '''Mutant:'''
  
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* '''Expression vector:''' pAG3 (His-tag), available in [[Galinier]] lab
+
* '''Expression vector:'''
−
+
       
 
* '''lacZ fusion:'''
 
* '''lacZ fusion:'''
  
 
* '''GFP fusion:'''
 
* '''GFP fusion:'''
 +
 +
* '''two-hybrid system:'''
  
 
* '''Antibody:'''
 
* '''Antibody:'''
  
 
=Labs working on this gene/protein=
 
=Labs working on this gene/protein=
−
 
−
[[Josef Deutscher]], Paris-Grignon, France
 
−
 
−
[[Stülke|Jörg Stülke]], University of Göttingen, Germany [http://wwwuser.gwdg.de/~genmibio/stuelke.html Homepage]
 
  
 
=Your additional remarks=
 
=Your additional remarks=
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=References=
 
=References=
  
−
<pubmed>12850135 17218307, </pubmed>
+
<pubmed>17218307, </pubmed>
−
# 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 [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed]
+
# Macek et al. (2007) The serine/ threonine/ tyrosine phosphoproteome of the model  bacterium ''Bacillus subtilis''. Mol. Cell. Proteomics 6: 697-707  [http://www.ncbi.nlm.nih.gov/pubmed/17218307 PubMed]
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# Frisby, D., and Zuber, P. 1994. Mutations in pts cause catabolite-resistant sporulation and altered regulation of spo0H in Bacillus subtilis. J. Bacteriol. 176: 2587-2595. [http://www.ncbi.nlm.nih.gov/sites/entrez/8169206  PubMed]
+
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]
−
# Macek B, Mijakovic I, Olsen JV (2007) The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis. ''Mol Cell Proteomics'' '''6(4):''' 697-707. [http://www.ncbi.nlm.nih.gov/sites/entrez/17218307 PubMed]
 

Revision as of 13:30, 8 June 2009

  • Description: purine nucleoside phosphorylase

Gene name punA
Synonyms pnp, yqkO
Essential no
Product purine nucleoside phosphorylase
Function purine salvage and interconversion
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



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:
  • Interactions:
  • Localization: secreted (according to Swiss-Prot)

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Operon:
  • Regulation:
  • 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

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)

  1. Macek et al. (2007) The serine/ threonine/ tyrosine phosphoproteome of the model bacterium Bacillus subtilis. Mol. Cell. Proteomics 6: 697-707 PubMed
  2. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed
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