Difference between revisions of "PdxT"
| Line 126: | Line 126: | ||
** number of protein molecules per cell (minimal medium with glucose and ammonium): 1683 {{PubMed|24696501}}  | ** number of protein molecules per cell (minimal medium with glucose and ammonium): 1683 {{PubMed|24696501}}  | ||
** number of protein molecules per cell (complex medium with amino acids, without glucose): 3958 {{PubMed|24696501}}  | ** number of protein molecules per cell (complex medium with amino acids, without glucose): 3958 {{PubMed|24696501}}  | ||
| + | ** number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 749 {{PubMed|21395229}}  | ||
| + | ** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 443 {{PubMed|21395229}}  | ||
| + | ** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 55 {{PubMed|21395229}}  | ||
=Biological materials =  | =Biological materials =  | ||
| − | |||
* '''Mutant:'''  | * '''Mutant:'''  | ||
Revision as of 14:16, 17 April 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  
  This image was kindly provided by SubtiList 
 | |
Expression at a glance   PubMed 
 | |
Contents
Categories containing this gene/protein
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU00120
 
Phenotypes of a mutant
Database entries
- BsubCyc: BSU00120
 
- 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
- BsubCyc: BSU00120
 
- UniProt: P37528
 
- KEGG entry: [3]
 
- E.C. number:
 
Additional information
Expression and regulation
-  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
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)

