NadB

• Description: L-aspartate oxidase
  
  

Gene name	nadB
Synonyms
Essential	no
Product	L-aspartate oxidase
Function	NAD biosynthesis
Gene expression levels in SubtiExpress: nadB
Metabolic function and regulation of this protein in SubtiPathways: 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

Categories containing this gene/protein

biosynthesis of cofactors, phosphoproteins

This gene is a member of the following regulons

NadR regulon

The gene

Basic information

• Locus tag: BSU27870

Database entries

• BsubCyc: BSU27870

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Interactions:

• Localization:

Database entries

• BsubCyc: BSU27870

• Structure:

• UniProt: P38032

• KEGG entry: [3]

• E.C. number: 1.4.3.16

Expression and regulation

• Operon: nadB-nadC-nadA PubMed

• Expression browser: nadB PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • repressed in the presence of nicotinic acid (NadR) PubMed

• Regulatory mechanism:
  • NadR: transcription repression PubMed

• 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

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)