Difference between revisions of "PdxT"
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# Molle et al. (2003) The Spo0A regulon of ''Bacillus subtilis''.''Mol. Microbiol.'' '''50:''' 1683-1701. [http://www.ncbi.nlm.nih.gov/sites/entrez/14651647 PubMed] | # Molle et al. (2003) The Spo0A regulon of ''Bacillus subtilis''.''Mol. Microbiol.'' '''50:''' 1683-1701. [http://www.ncbi.nlm.nih.gov/sites/entrez/14651647 PubMed] | ||
# Raschle et al. (2005) On the two components of pyridoxal 5'-phosphate synthase from ''Bacillus subtilis''.''J. Biol. Chem.'' '''280:''' 32291-32300. [http://www.ncbi.nlm.nih.gov/sites/entrez/16030023 PubMed] | # Raschle et al. (2005) On the two components of pyridoxal 5'-phosphate synthase from ''Bacillus subtilis''.''J. Biol. Chem.'' '''280:''' 32291-32300. [http://www.ncbi.nlm.nih.gov/sites/entrez/16030023 PubMed] | ||
# Belitsky (2004) Physical and enzymological interaction of ''Bacillus subtilis'' proteins required for ''de novo'' pyridoxal 5'-phosphate biosynthesis.''J. Bacteriol.'' '''186:''' 1191-1196. [http://www.ncbi.nlm.nih.gov/sites/entrez/14762015 PubMed] | # Belitsky (2004) Physical and enzymological interaction of ''Bacillus subtilis'' proteins required for ''de novo'' pyridoxal 5'-phosphate biosynthesis.''J. Bacteriol.'' '''186:''' 1191-1196. [http://www.ncbi.nlm.nih.gov/sites/entrez/14762015 PubMed] |
Revision as of 18:47, 22 May 2009
- 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 |
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 This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Coordinates:
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:
- Localization:
Database entries
- Swiss prot entry: P37528
- KEGG entry: BSU00120
- E.C. number:
Additional information
Expression and regulation
- 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)
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)
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)
- Molle et al. (2003) The Spo0A regulon of Bacillus subtilis.Mol. Microbiol. 50: 1683-1701. PubMed
- Raschle et al. (2005) On the two components of pyridoxal 5'-phosphate synthase from Bacillus subtilis.J. Biol. Chem. 280: 32291-32300. PubMed
- Belitsky (2004) Physical and enzymological interaction of Bacillus subtilis proteins required for de novo pyridoxal 5'-phosphate biosynthesis.J. Bacteriol. 186: 1191-1196. PubMed