SdaAA

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  • Description: L-serine deaminase

Gene name sdaAA
Synonyms ylpA, sdaA
Essential no
Product L-serine deaminase (alpha chain)
Function serine utilization
Metabolic function and regulation of this protein in SubtiPathways:
Ala, Gly, Ser
MW, pI 30 kDa, 4.87
Gene length, protein length 900 bp, 300 aa
Immediate neighbours sdaAB, recG
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
SdaAA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
SdaAA expression.png




























Categories containing this gene/protein

utilization of amino acids

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU15860

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: L-serine = pyruvate + NH3 (according to Swiss-Prot)
  • Protein family: iron-sulfur dependent L-serine dehydratase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s): iron-sulfur cluster PubMed
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [2]

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

Shawei Chen, Xiao Lan Xu, Gregory A Grant
Allosteric activation and contrasting properties of L-serine dehydratase types 1 and 2.
Biochemistry: 2012, 51(26);5320-8
[PubMed:22686449] [WorldCat.org] [DOI] (I p)

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)