Difference between revisions of "MoaE"

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(Original publications)
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<pubmed> 22616866 </pubmed>
 
<pubmed> 22616866 </pubmed>
 
== Original publications ==
 
== Original publications ==
<pubmed> 12571227 </pubmed>
+
<pubmed> 12571227 22383849</pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 14:37, 4 June 2012

  • Description: molybdopterin synthase (large subunit), catalyses the transfer of sulfide from MoaD thiocarboxylate

Gene name moaE
Synonyms
Essential no
Product molybdopterin synthase (large subunit)
Function nitrate respiration
MW, pI 17 kDa, 4.746
Gene length, protein length 471 bp, 157 aa
Immediate neighbours mobB, moaD
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
MoaE context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
MoaE expression.png
























Categories containing this gene/protein

biosynthesis of cofactors

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU14300

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: catalyses the transfer of sulfide from MoaD thiocarboxylate
  • Protein family: moaE 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: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Sigma factor:
  • Regulation:
  • Regulatory mechanism:
  • 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

Reviews

Tadhg P Begley, Steven E Ealick, Fred W McLafferty
Thiamin biosynthesis: still yielding fascinating biological chemistry.
Biochem Soc Trans: 2012, 40(3);555-60
[PubMed:22616866] [WorldCat.org] [DOI] (I p)

Original publications

Pierre Nicolas, Ulrike Mäder, Etienne Dervyn, Tatiana Rochat, Aurélie Leduc, Nathalie Pigeonneau, Elena Bidnenko, Elodie Marchadier, Mark Hoebeke, Stéphane Aymerich, Dörte Becher, Paola Bisicchia, Eric Botella, Olivier Delumeau, Geoff Doherty, Emma L Denham, Mark J Fogg, Vincent Fromion, Anne Goelzer, Annette Hansen, Elisabeth Härtig, Colin R Harwood, Georg Homuth, Hanne Jarmer, Matthieu Jules, Edda Klipp, Ludovic Le Chat, François Lecointe, Peter Lewis, Wolfram Liebermeister, Anika March, Ruben A T Mars, Priyanka Nannapaneni, David Noone, Susanne Pohl, Bernd Rinn, Frank Rügheimer, Praveen K Sappa, Franck Samson, Marc Schaffer, Benno Schwikowski, Leif Steil, Jörg Stülke, Thomas Wiegert, Kevin M Devine, Anthony J Wilkinson, Jan Maarten van Dijl, Michael Hecker, Uwe Völker, Philippe Bessières, Philippe Noirot
Condition-dependent transcriptome reveals high-level regulatory architecture in Bacillus subtilis.
Science: 2012, 335(6072);1103-6
[PubMed:22383849] [WorldCat.org] [DOI] (I p)

Michael J Rudolph, Margot M Wuebbens, Oliver Turque, K V Rajagopalan, Hermann Schindelin
Structural studies of molybdopterin synthase provide insights into its catalytic mechanism.
J Biol Chem: 2003, 278(16);14514-22
[PubMed:12571227] [WorldCat.org] [DOI] (P p)