Difference between revisions of "PdxS"

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* '''Structure:'''  
 
* '''Structure:'''  
** [http://www.rcsb.org/pdb/explore.do?structureId=2NV1 2NV1] [[PdxS]]
+
** [http://www.rcsb.org/pdb/explore.do?structureId=2NV1 2NV1] [[PdxS]] {{PubMed|17159152}}
** [http://www.rcsb.org/pdb/explore.do?structureId=2NV2 2NV2] [[PdxS]]-[[PdxT]] complex  
+
** [http://www.rcsb.org/pdb/explore.do?structureId=2NV2 2NV2] [[PdxS]]-[[PdxT]] complex {{PubMed|17159152}}
  
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P37527 P37527]
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P37527 P37527]
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=pdxS_19062_19946_1 pdxS] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=pdxS_19062_19946_1 pdxS] {{PubMed|22383849}}
  
* '''Sigma factor:'''  
+
* '''[[Sigma factor]]:'''  
  
 
* '''Regulation:''' negatively controlled by [[Spo0A]] [http://www.ncbi.nlm.nih.gov/sites/entrez/14651647 PubMed]
 
* '''Regulation:''' negatively controlled by [[Spo0A]] [http://www.ncbi.nlm.nih.gov/sites/entrez/14651647 PubMed]
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=References=
 
=References=
  
<pubmed>15911615,14762015,,14651647, 17726680, 16493705, 14651647, 16030023, 14762015, 19152323,17159152 22517742 </pubmed>
+
<pubmed>15911615,14762015,,14651647, 17726680, 16493705, 16030023, 19152323,17159152 22517742 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 07:55, 9 July 2013

  • Description: pyridoxal-5'-phosphate synthase (synthase domain)

Gene name pdxS
Synonyms yaaD
Essential no
Product pyridoxal-5'-phosphate synthase (synthase domain)
Function pyridoxal-5'-phosphate biosynthesis
Gene expression levels in SubtiExpress: pdxS
Interactions involving this protein in SubtInteract: PdxS
MW, pI 31 kDa, 5.085
Gene length, protein length 882 bp, 294 aa
Immediate neighbours dacA, pdxT
Sequences Protein DNA DNA_with_flanks
Genetic context
YaaD context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
PdxS expression.png















Categories containing this gene/protein

biosynthesis of cofactors, phosphoproteins

This gene is a member of the following regulons

Spo0A regulon

The gene

Basic information

  • Locus tag: BSU00110

Phenotypes of a mutant

auxotrophic for pyridoxal 5'-phosphate PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: pdxS/SNZ family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation: negatively controlled by Spo0A PubMed
    • repressed under conditions that trigger sporulation (Spo0A) 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

Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742] [WorldCat.org] [DOI] (I p)

Silvia Wallner, Martina Neuwirth, Karlheinz Flicker, Ivo Tews, Peter Macheroux
Dissection of contributions from invariant amino acids to complex formation and catalysis in the heteromeric pyridoxal 5-phosphate synthase complex from Bacillus subtilis.
Biochemistry: 2009, 48(9);1928-35
[PubMed:19152323] [WorldCat.org] [DOI] (I p)

Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680] [WorldCat.org] [DOI] (P p)

Marco Strohmeier, Thomas Raschle, Jacek Mazurkiewicz, Karsten Rippe, Irmgard Sinning, Teresa B Fitzpatrick, Ivo Tews
Structure of a bacterial pyridoxal 5'-phosphate synthase complex.
Proc Natl Acad Sci U S A: 2006, 103(51);19284-9
[PubMed:17159152] [WorldCat.org] [DOI] (P p)

Alain Lévine, Françoise Vannier, Cédric Absalon, Lauriane Kuhn, Peter Jackson, Elaine Scrivener, Valérie Labas, Joëlle Vinh, Patrick Courtney, Jérôme Garin, Simone J Séror
Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes.
Proteomics: 2006, 6(7);2157-73
[PubMed:16493705] [WorldCat.org] [DOI] (P p)

Thomas Raschle, Nikolaus Amrhein, Teresa B Fitzpatrick
On the two components of pyridoxal 5'-phosphate synthase from Bacillus subtilis.
J Biol Chem: 2005, 280(37);32291-300
[PubMed:16030023] [WorldCat.org] [DOI] (P p)

Jianghai Zhu, John W Burgner, Etti Harms, Boris R Belitsky, Janet L Smith
A new arrangement of (beta/alpha)8 barrels in the synthase subunit of PLP synthase.
J Biol Chem: 2005, 280(30);27914-23
[PubMed:15911615] [WorldCat.org] [DOI] (P p)

Boris R Belitsky
Physical and enzymological interaction of Bacillus subtilis proteins required for de novo pyridoxal 5'-phosphate biosynthesis.
J Bacteriol: 2004, 186(4);1191-6
[PubMed:14762015] [WorldCat.org] [DOI] (P p)

Virginie Molle, Masaya Fujita, Shane T Jensen, Patrick Eichenberger, José E González-Pastor, Jun S Liu, Richard Losick
The Spo0A regulon of Bacillus subtilis.
Mol Microbiol: 2003, 50(5);1683-701
[PubMed:14651647] [WorldCat.org] [DOI] (P p)