Difference between revisions of "PdxS"
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|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 882 bp, 294 aa | |style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 882 bp, 294 aa | ||
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− | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || | + | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[dacA]]'', ''[[pdxT]]'' |
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|style="background:#FAF8CC;" align="center"|'''[http://subtiwiki.uni-goettingen.de/yaaD_nucleotide.txt Gene sequence (+200bp) ]''' | |style="background:#FAF8CC;" align="center"|'''[http://subtiwiki.uni-goettingen.de/yaaD_nucleotide.txt Gene sequence (+200bp) ]''' |
Revision as of 13:38, 20 February 2009
- Description: subunit of pyridoxal-5'-phosphate synthase
Gene name | pdxS |
Synonyms | yaaD |
Essential | no |
Product | synthase domain of pyridoxal-5'-phosphate synthase |
Function | unknown |
MW, pI | 31 kDa, 5.085 |
Gene length, protein length | 882 bp, 294 aa |
Immediate neighbours | dacA, pdxT |
Gene sequence (+200bp) | Protein sequence |
Genetic context |
Contents
The gene
Basic information
- Coordinates:
Phenotypes of a mutant
auxotrophic for pyridoxal 5'-phosphate PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification: phosphorylated on STY PubMed
- Cofactor(s):
- Effectors of protein activity:
- Localization:
Database entries
- Swiss prot entry:
- KEGG entry:
- E.C. number:
Additional information
Expression and regulation
- Sigma factor:
- 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
- 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
- Levine et al. (2006) Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of celular processes. Proteomics 6, 2157-2173. PubMed