Difference between revisions of "NadB"
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Revision as of 14:08, 16 May 2013
- Description: L-aspartate oxidase
| Gene name | nadB |
| Synonyms | |
| Essential | no |
| Product | L-aspartate oxidase |
| Function | NAD biosynthesis |
| Gene expression levels in SubtiExpress: nadB | |
| MW, pI | 58 kDa, 6.445 |
| Gene length, protein length | 1593 bp, 531 aa |
| Immediate neighbours | nadC, nifS |
| 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
biosynthesis of cofactors, phosphoproteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU27870
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: L-aspartate + O2 = iminosuccinate + H2O2 (according to Swiss-Prot)
- Protein family: NadB subfamily (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- phosphorylated on Arg-104 PubMed
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure:
- UniProt: P38032
- KEGG entry: [3]
- E.C. number: 1.4.3.16
Additional information
Expression and regulation
- Additional information:
- An antisense RNA is predicted for nadB PubMed
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
Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742]
[WorldCat.org]
[DOI]
(I p)
Irnov Irnov, Cynthia M Sharma, Jörg Vogel, Wade C Winkler
Identification of regulatory RNAs in Bacillus subtilis.
Nucleic Acids Res: 2010, 38(19);6637-51
[PubMed:20525796]
[WorldCat.org]
[DOI]
(I p)
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)
