SdaAB

• Description: L-serine deaminase
  
  

Gene name	sdaAB
Synonyms	yloW, sdaA
Essential	no
Product	L-serine deaminase (beta chain)
Function	serine utilization
Gene expression levels in SubtiExpress: sdaAB
Metabolic function and regulation of this protein in SubtiPathways: sdaAB
MW, pI	23 kDa, 5.103
Gene length, protein length	660 bp, 220 aa
Immediate neighbours	yloV, sdaAA
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

utilization of amino acids

The gene

Basic information

• Locus tag: BSU15850

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: L-serine = pyruvate + NH₃ (according to Swiss-Prot)

• Protein family: ACT domain (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • SdaAA-SdaAB PubMed

• Localization:

Database entries

• Structure:

• UniProt: O34635

• KEGG entry: [2]

• E.C. number: 4.3.1.17

Expression and regulation

• Operon: sdaAB-sdaAA PubMed

• Expression browser: sdaAB PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Xiao Lan Xu, Gregory A Grant
Identification and characterization of two new types of bacterial L-serine dehydratases and assessment of the function of the ACT domain.
Arch Biochem Biophys: 2013, 540(1-2);62-9
[PubMed:24161940] [WorldCat.org] [DOI] (I p)

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)