SerA

• Description: phosphoglycerate dehydrogenase
  
  

Gene name	serA
Synonyms
Essential	no
Product	phosphoglycerate dehydrogenase
Function	biosynthesis of serine
Gene expression levels in SubtiExpress: serA
Metabolic function and regulation of this protein in SubtiPathways: serA
MW, pI	56 kDa, 5.617
Gene length, protein length	1575 bp, 525 aa
Immediate neighbours	ypzE, aroC
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

biosynthesis/ acquisition of amino acids, membrane proteins, most abundant proteins

The gene

Basic information

• Locus tag: BSU23070

Database entries

• BsubCyc: BSU23070

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: 3-phospho-D-glycerate + NAD⁺ = 3-phosphonooxypyruvate + NADH (according to Swiss-Prot)

• Protein family: D-isomer specific 2-hydroxyacid dehydrogenase family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:
  • S-cysteinylation after diamide stress (C410)PubMed
  • active site Cys410 is S-bacillithiolated by NaOCl stress in B. subtilis and other Bacillus species PubMed PubMed

• Cofactors:

• Effectors of protein activity:

• Interactions:

• Localization: membrane PubMed

Database entries

• BsubCyc: BSU23070

• Structure: 1YBA (from E. coli, 30% identity, 52% similarity) PubMed

• UniProt: P35136

• KEGG entry: [3]

• E.C. number: 1.1.1.95

Expression and regulation

• Operon: serA PubMed

• Expression browser: serA PubMed

• Sigma factor:

• Regulation:
  • strongly repressed in response to glucose starvation in M9 medium PubMed

• Regulatory mechanism:

• Additional information:
  • belongs to the 100 most abundant proteins PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 6336 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 12316 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 9076 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 4149 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 5497 PubMed

Biological materials

• Mutant:
  • 1A614 ( serA::erm), PubMed, available at BGSC

• Expression vector:

• lacZ fusion: pGP187 (in pAC7), available in Stülke lab

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Imke G de Jong, Jan-Willem Veening, Oscar P Kuipers
Single cell analysis of gene expression patterns during carbon starvation in Bacillus subtilis reveals large phenotypic variation.
Environ Microbiol: 2012, 14(12);3110-21
[PubMed:23033921] [WorldCat.org] [DOI] (I p)

Bui Khanh Chi, Alexandra A Roberts, Tran Thi Thanh Huyen, Katrin Bäsell, Dörte Becher, Dirk Albrecht, Chris J Hamilton, Haike Antelmann
S-bacillithiolation protects conserved and essential proteins against hypochlorite stress in firmicutes bacteria.
Antioxid Redox Signal: 2013, 18(11);1273-95
[PubMed:22938038] [WorldCat.org] [DOI] (I p)

Bui Khanh Chi, Katrin Gronau, Ulrike Mäder, Bernd Hessling, Dörte Becher, Haike Antelmann
S-bacillithiolation protects against hypochlorite stress in Bacillus subtilis as revealed by transcriptomics and redox proteomics.
Mol Cell Proteomics: 2011, 10(11);M111.009506
[PubMed:21749987] [WorldCat.org] [DOI] (I p)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I p)

Falko Hochgräfe, Jörg Mostertz, Dierk-Christoph Pöther, Dörte Becher, John D Helmann, Michael Hecker
S-cysteinylation is a general mechanism for thiol protection of Bacillus subtilis proteins after oxidative stress.
J Biol Chem: 2007, 282(36);25981-5
[PubMed:17611193] [WorldCat.org] [DOI] (P p)

James R Thompson, Jessica K Bell, Judy Bratt, Gregory A Grant, Leonard J Banaszak
Vmax regulation through domain and subunit changes. The active form of phosphoglycerate dehydrogenase.
Biochemistry: 2005, 44(15);5763-73
[PubMed:15823035] [WorldCat.org] [DOI] (P p)

Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759] [WorldCat.org] [DOI] (P p)

V Azevedo, A Sorokin, S D Ehrlich, P Serror
The transcriptional organization of the Bacillus subtilis 168 chromosome region between the spoVAF and serA genetic loci.
Mol Microbiol: 1993, 10(2);397-405
[PubMed:7934830] [WorldCat.org] [DOI] (P p)