Difference between revisions of "SerA"

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= Categories containing this gene/protein =
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{{SubtiWiki category|[[biosynthesis/ acquisition of amino acids]]}},
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{{SubtiWiki category|[[membrane proteins]]}}
 
=The protein=
 
=The protein=
  

Revision as of 19:50, 30 November 2010

  • Description: phosphoglycerate dehydrogenase

Gene name serA
Synonyms
Essential no
Product phosphoglycerate dehydrogenase
Function biosynthesis of serine
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
SerA context.gif
This image was kindly provided by SubtiList







The gene

Basic information

  • Locus tag: BSU23070

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

Categories containing this gene/protein

biosynthesis/ acquisition of amino acids, membrane proteins

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
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization: membrane PubMed

Database entries

  • Structure: 1YBA (from E. coli, 30% identity, 52% similarity) PubMed
  • KEGG entry: [3]

Additional information

Expression and regulation

  • 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:

Labs working on this gene/protein

Your additional remarks

References

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)