Difference between revisions of "YhdA"

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Revision as of 12:51, 16 May 2013

  • Description: similar to NADPH-dependent azobenzene FMN reductase

Gene name yhdA
Synonyms
Essential no
Product unknown
Function unknown
Gene expression levels in SubtiExpress: yhdA
MW, pI 18 kDa, 6.508
Gene length, protein length 522 bp, 174 aa
Immediate neighbours yhcZ, yhdB
Sequences Protein DNA DNA_with_flanks
Genetic context
YhdA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
YhdA expression.png


























Categories containing this gene/protein

poorly characterized/ putative enzymes

This gene is a member of the following regulons

LiaR regulon

The gene

Basic information

  • Locus tag: BSU09340

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: azoreductase type 2 family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism: LiaR: transcription activation PubMed
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

K Ramanathan, V Shanthi, Rao Sethumadhavan
In silico identification of catalytic residues in azobenzene reductase from Bacillus subtilis and its docking studies with azo dyes.
Interdiscip Sci: 2009, 1(4);290-7
[PubMed:20640807] [WorldCat.org] [DOI] (P p)

Diana Wolf, Falk Kalamorz, Tina Wecke, Anna Juszczak, Ulrike Mäder, Georg Homuth, Sina Jordan, Janine Kirstein, Michael Hoppert, Birgit Voigt, Michael Hecker, Thorsten Mascher
In-depth profiling of the LiaR response of Bacillus subtilis.
J Bacteriol: 2010, 192(18);4680-93
[PubMed:20639339] [WorldCat.org] [DOI] (I p)

Sina Jordan, Anja Junker, John D Helmann, Thorsten Mascher
Regulation of LiaRS-dependent gene expression in bacillus subtilis: identification of inhibitor proteins, regulator binding sites, and target genes of a conserved cell envelope stress-sensing two-component system.
J Bacteriol: 2006, 188(14);5153-66
[PubMed:16816187] [WorldCat.org] [DOI] (P p)