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pdhA [Thu Oct 01 2015 13:51:44 GMT+0200 (CEST)]
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pdhA [Thu Oct 01 2015 13:51:44 GMT+0200 (CEST)]

pyruvate dehydrogenase (E1 alpha subunit), required for Z-ring assembly in a pyruvate-dependent manner
locus
BSU14580
pI
5.00
mw
41.00 kDa
function
links glycolysis and TCA cycle
product
pyruvate dehydrogenase (E1 alpha subunit)
essential
yes
ec
1.2.4.1
synonyms
aceA

Genomic Context

      

categories

  • [category|SW 2|Metabolism] → [category|SW 2.2|Carbon metabolism] → [category|SW 2.2.1|Carbon core metabolism] → [category|SW 2.2.1.4|TCA cycle]
  • [SW|Categories] containing this gene/protein

  • [SW|carbon core metabolism], [SW|essential genes], [SW|most abundant proteins]
  • This gene is a member of the following [SW|regulons]

  • [SW|stringent response]
  • Gene

    Coordinates on the chromosome (coding sequence)
    1,528,326 -> 1,529,441

    Phenotypes of a mutant

  • ''pdhA'' is essential according to Kobayashi ''et al''. [Pubmed|12682299]
  • the mutant grows slowly but is viable [Pubmed|24825009]
  • depletion of ''[protein|search|pdhA]'' and deletion of ''[protein|search|ezrA]'' have a strong synthetic defect in [SW|cell division] [Pubmed|24825009]
  • The protein

    Catalyzed reaction/ biological activity

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

  • [protein|search|AcoA], [SW|BkdAA]
  • Kinetic information

  • Michaelis-Menten [Pubmed|6414463]
  • [SW|Cofactors]

  • thiamine pyrophosphate
  • Effectors of protein activity

  • Inhibited thiamine 2-thiothiazolone diphosphate and NADH [Pubmed|6414463]
  • Low sensibility to NADPH
  • Structure

  • [PDB|1W88] (E1 in complex with subunit binding domain of E2, ''Geobacillus stearothermophilus'')
  • [SW|Localization]

  • colocalizes with the nucleoid (depending on the availability of pyruvate) [Pubmed|24825009]
  • [SW|Interactions]

  • [protein|search|PdhA]-[protein|search|PdhB]-[protein|search|PdhC]-[protein|search|PdhD]
  • Expression and Regulation

    Operon

  • ''[protein|search|pdhA]-[protein|search|pdhB]-[protein|search|pdhC]-[protein|search|pdhD]'' [Pubmed|11976308]
  • [SW|Sigma factor]

  • [protein|search|SigA] [Pubmed|20081037]
  • Regulation

  • expression activated by glucose (3.4) [Pubmed|12850135]
  • subject to negative stringent control upon amino acid limitation [Pubmed|20081037]
  • Regulatory mechanism

  • stringent response: due to presence of guanine at 1 position of the transcript [Pubmed|20081037]
  • Biological materials

    lacZ fusion

  • pGP721 (in [protein|search|pAC5]), available in [SW|Stülke] lab, pGP186 (in [protein|search|pAC7]), available in [SW|Stülke] lab
  • Labs working on this gene/protein

  • [SW|Arthur Aronson], Purdue University, West Lafayette, USA [http://wwwdev.gradschool.purdue.edu/PULSe/faculty.cfm?fid=5&range=0 homepage]
  • References

    Reviews

  • 19476487,9655937,2227213,6805383,24798336
  • Original publications

  • 9352926,20525796,12850135,6414463,11976308,20081037,15378759,24825009