Difference between revisions of "PdxT"

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=== Additional information===
 
=== Additional information===
 
 
 
  
 
=The protein=
 
=The protein=
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* '''[[SubtInteract|Interactions]]:'''
 
* '''[[SubtInteract|Interactions]]:'''
**  [[PdxS]]-[[PdxT]] [http://www.ncbi.nlm.nih.gov/sites/entrez/16030023 PubMed1] [http://www.ncbi.nlm.nih.gov/sites/entrez/14762015 PubMed2]
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**  [[PdxS]]-[[PdxT]] {{PubMed|25473090,14762015,16030023,17159152}}
  
 
* '''[[Localization]]:'''
 
* '''[[Localization]]:'''
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=References=
 
=References=
  
<pubmed>15911615,14762015,14651647 16030023, 19152323,17159152 23832367 </pubmed>
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<pubmed>15911615,14762015,14651647 16030023, 19152323,17159152 23832367 25473090</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 09:27, 5 December 2014

  • 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
Gene expression levels in SubtiExpress: pdxT
Interactions involving this protein in SubtInteract: PdxT
Metabolic function and regulation of this protein in SubtiPathways:
PdxT
MW, pI 21 kDa, 4.984
Gene length, protein length 588 bp, 196 aa
Immediate neighbours pdxS, serS
Sequences Protein DNA DNA_with_flanks
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

  • Regulation: negatively controlled by Spo0A PubMed
    • repressed under conditions that trigger sporulation (Spo0A) PubMed
  • Regulatory mechanism:
  • Additional information:
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 1683 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 3958 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 749 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 443 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 55 PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Miriam Dormeyer, Richard Egelkamp, Martin J Thiele, Elke Hammer, Katrin Gunka, Lorena Stannek, Uwe Völker, Fabian M Commichau
A novel engineering tool in the Bacillus subtilis toolbox: inducer-free activation of gene expression by selection-driven promoter decryptification.
Microbiology (Reading): 2015, 161(Pt 2);354-361
[PubMed:25473090] [WorldCat.org] [DOI] (I p)

Shiori Itagaki, Minami Haga, Yuji Oikawa, Ayaka Sakoda, Yoshie Ohke, Hiroshi Sawada, Tadashi Eguchi, Hideyuki Tamegai
Differences in the roles of a glutamine amidotransferase subunit of pyridoxal 5'-phosphate synthase between Bacillus circulans and Bacillus subtilis.
Biosci Biotechnol Biochem: 2013, 77(7);1481-5
[PubMed:23832367] [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)

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)