Difference between revisions of "NadB"

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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[nadC]]'', ''[[nifS]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[nadC]]'', ''[[nifS]]''
 
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU27870 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU27870 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU27870 Advanced_DNA]
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU27870 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU27870 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU27870 DNA_with_flanks]
 
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|colspan="2" | '''Genetic context''' <br/> [[Image:nadB_context.gif]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:nadB_context.gif]]

Revision as of 10:53, 14 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
NadB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
NadB expression.png
























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

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:
  • KEGG entry: [3]

Additional information

Expression and regulation

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

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)