PdxS

• 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
MW, pI	31 kDa, 5.085
Gene length, protein length	882 bp, 294 aa
Immediate neighbours	dacA, pdxT
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

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]

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:

• Modification: phosphorylated on STY PubMed, PubMed

• Cofactor(s):

• Effectors of protein activity:

• Interactions: PdxS-PdxT PubMed1 PubMed2

• Localization:

Database entries

• Structure: 2NV2 PdxS-PdxT complex

• UniProt: P37527

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: pdxS-pdxT

• Sigma factor:

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

• Regulatory mechanism:
  • Spo0A: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

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)