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: Ala, Gly, Ser
MW, pI	56 kDa, 5.617
Gene length, protein length	1575 bp, 525 aa
Immediate neighbours	ypzE, aroC
Get the DNA and protein sequences (Barbe et al., 2009)
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

The gene

Basic information

• Locus tag: BSU23070

Database entries

• 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

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization: membrane PubMed

Database entries

• 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:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

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

• GFP fusion:

• two-hybrid system:

• Antibody:

References

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)

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)