Difference between revisions of "NadA"
m (Reverted edits by 134.76.70.252 (talk) to last revision by Jstuelk)  | 
				|||
| Line 97: | Line 97: | ||
* '''Operon:''' ''[[nadB]]-[[nadC]]-[[nadA]]'' {{PubMed|8444804}}    | * '''Operon:''' ''[[nadB]]-[[nadC]]-[[nadA]]'' {{PubMed|8444804}}    | ||
| − | * '''[  | + | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=nadA_2845955_2847061_-1 nadA] {{PubMed|22383849}}  | 
| + | |||
| + | * '''Sigma factor:''' [[SigA]] {{PubMed|8444804}}    | ||
* '''Regulation:'''    | * '''Regulation:'''    | ||
| Line 105: | Line 107: | ||
** [[NadR]]: transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/16199587 PubMed]  | ** [[NadR]]: transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/16199587 PubMed]  | ||
| − | * '''Additional information:'''    | + | * '''Additional information:'''  | 
=Biological materials =  | =Biological materials =  | ||
Revision as of 14:16, 16 April 2012
-  Description: quinolinate synthetase 
 
| Gene name | nadA | 
| Synonyms | |
| Essential | no | 
| Product | quinolinate synthetase | 
| Function | NAD biosynthesis | 
| MW, pI | 41 kDa, 5.717 | 
| Gene length, protein length | 1104 bp, 368 aa | 
| Immediate neighbours | safA, nadC | 
| Get the DNA and protein sequences  (Barbe et al., 2009)  | |
 Genetic context  
  This image was kindly provided by SubtiList 
 | |
Contents
Categories containing this gene/protein
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU27850
 
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
 
- SubtiList entry: [2]
 
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Glycerone phosphate + iminosuccinate = pyridine-2,3-dicarboxylate + 2 H2O + phosphate (according to Swiss-Prot)
 
- Protein family: Type 3 subfamily (according to Swiss-Prot)
 
- Paralogous protein(s):
 
Extended information on the protein
- Kinetic information:
 
- Domains:
 
- Modification:
 
- Cofactor(s):
 
- Effectors of protein activity:
 
Database entries
- Structure:
 
- UniProt: Q9KWZ1
 
- KEGG entry: [3]
 
- E.C. number: 2.5.1.72
 
Additional information
Expression and regulation
- Additional information:
 
Biological materials
- Mutant:
 
- Expression vector:
 
- lacZ fusion:
 
- GFP fusion:
 
- two-hybrid system:
 
- Antibody:
 
Labs working on this gene/protein
Alessandra Albertini, University of Pavia, Italy homepage
Your additional remarks
References
Ilaria Marinoni, Simona Nonnis, Carmine Monteferrante, Peter Heathcote, Elisabeth Härtig, Lars H Böttger, Alfred X Trautwein, Armando Negri, Alessandra M Albertini, Gabriella Tedeschi  
Characterization of L-aspartate oxidase and quinolinate synthase from Bacillus subtilis. 
FEBS J: 2008, 275(20);5090-107 
[PubMed:18959769]
  [WorldCat.org]
 [DOI]
 (I p)
Paola Rossolillo, Ilaria Marinoni, Elisa Galli, Anna Colosimo, Alessandra M Albertini  
YrxA is the transcriptional regulator that represses de novo NAD biosynthesis in Bacillus subtilis. 
J Bacteriol: 2005, 187(20);7155-60 
[PubMed:16199587]
  [WorldCat.org]
 [DOI]
 (P p)
D Sun, P Setlow  
Cloning, nucleotide sequence, and regulation of the Bacillus subtilis nadB gene and a nifS-like gene, both of which are essential for NAD biosynthesis. 
J Bacteriol: 1993, 175(5);1423-32 
[PubMed:8444804]
  [WorldCat.org]
 [DOI]
 (P p)
