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pdhA [Mon Jan 18 2016 15:29:09 GMT+0100 (CET)]
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pdhA [Mon Jan 18 2016 15:29:09 GMT+0100 (CET)]

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
Outlinks
KEGGBsubCycSubtiListUniProtExpression Browser

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]

    • Additional information

  • belongs to the 100 [SW|most abundant proteins] [PubMed|15378759]

    • 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