Difference between revisions of "PdxT"

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Revision as of 12:13, 18 April 2012

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

Gene name pdxT
Synonyms yaaE
Essential no
Product pyridoxal-5'-phosphate synthase (glutaminase domain)
Function pyridoxal-5'-phosphate biosynthesis
Interactions involving this protein in SubtInteract: PdxT
MW, pI 21 kDa, 4.984
Gene length, protein length 588 bp, 196 aa
Immediate neighbours pdxS, serS
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YaaE context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
PdxT expression.png
























Categories containing this gene/protein

biosynthesis of cofactors

This gene is a member of the following regulons

Spo0A regulon

The gene

Basic information

  • Locus tag: BSU00120

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: glutamine amidotransferase pdxT/SNO family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

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

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Sigma factor:
  • 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

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)

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)

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)