Difference between revisions of "NadA"
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=Expression and regulation= | =Expression and regulation= | ||
+ | * '''Operon:''' ''[[nadB]]-[[nadC]]-[[nadA]]'' {{PubMed|8444804}} | ||
− | + | * '''[[Sigma factor]]:''' [[SigA]] {{PubMed|8444804}} | |
− | |||
− | * '''[[Sigma factor]]:''' | ||
* '''Regulation:''' | * '''Regulation:''' | ||
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=References= | =References= | ||
− | <pubmed>18959769,16199587,, | + | <pubmed>18959769,16199587,,8444804, </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 20:04, 26 November 2009
- 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
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:
- Interactions:
- Localization: spore wall (according to Swiss-Prot)
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)