SubtiBank SubtiBank
pdhA [2019-02-24 17:45:36]
You are currently viewing an outdated version of SubtiWiki. Please use the newest version!

pdhA [2019-02-24 17:45:36]

pyruvate dehydrogenase (E1 alpha subunit), required for Z-ring assembly in a pyruvate-dependent manner
Locus
BSU14580
Isoelectric point
5.84
Molecular weight
41.39 kDa
Protein length
371 aa Sequence Blast
Gene length
1116 bp Sequence Blast
Function
links glycolysis and TCA cycle
Product
pyruvate dehydrogenase (E1 alpha subunit)
Essential
no
E.C.
1.2.4.1
Synonyms
aceA

Genomic Context

      
Loading

Categories containing this gene/protein

Gene

Coordinates
1,528,326 1,529,441

Phenotypes of a mutant

  • pdhA is essential according to Kobayashi et al. PubMed, non-essential according to PubMed
  • the mutant grows slowly but is viable PubMed
  • depletion of pdhA and deletion of ezrA have a strong synthetic defect in cell division PubMed
  • The protein

    Catalyzed reaction/ biological activity

  • Pyruvate [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine CO2 (according to Swiss-Prot)
  • Paralogous protein(s)

    Kinetic information

  • Michaelis-Menten PubMed
  • Cofactors

  • thiamine pyrophosphate
  • Effectors of protein activity

  • Inhibited thiamine 2-thiothiazolone diphosphate and NADH PubMed
  • Low sensibility to NADPH
  • Structure

  • 1W88 (E1 in complex with subunit binding domain of E2, Geobacillus stearothermophilus)
  • Localization

  • colocalizes with the nucleoid (depending on the availability of pyruvate) PubMed
  • Additional information

  • belongs to the 100 most abundant proteins PubMed
  • Expression and Regulation

    Operons

    Description

    Sigma factors

  • SigA: sigma factor, PubMed, in SigA regulon
  • Regulatory mechanism

  • stringent response: negative regulation, due to presence of guanine at 1 position of the transcript PubMed, in stringent response
  • Regulation

  • pdhA: expression activated by glucose (1.9-fold) PubMed
  • view in new tab

    Biological materials

    Mutant

  • BKE14580 (pdhA::erm trpC2) available at BGSC, PubMed, upstream reverse: _UP1_CATACTAAGTCACCTCTTCC, downstream forward: _UP4_ACACAGAAGGAGTCGAAGTA
  • BKK14580 (pdhA::kan trpC2) available at BGSC, PubMed, upstream reverse: _UP1_CATACTAAGTCACCTCTTCC, downstream forward: _UP4_ACACAGAAGGAGTCGAAGTA
  • LacZ fusion

  • pGP721 (in pAC5), available in Jörg Stülke's lab, pGP186 (in pAC7), available in Jörg Stülke's lab
  • Labs working on this gene/protein

  • Arthur Aronson, Purdue University, West Lafayette, USA homepage
  • References

    Reviews

    Loading

    Original publications

    Loading