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pdhC [2017-8-11 16:0:3]
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pdhC [2017-8-11 16:0:3]

pyruvate dehydrogenase (dihydrolipoamide acetyltransferase E2 subunit)
locus
BSU14600
pI
4.86
mw
47.38 kDa
protein length
442 aa Sequence Blast
gene length
1326 bp Sequence Blast
function
links glycolysis and TCA cycle
product
pyruvate dehydrogenase (dihydrolipoamide acetyltransferase E2 subunit)
essential
no
ec
2.3.1.12
synonyms
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]
  • [category|SW 3|Information processing] → [category|SW 3.1|Genetics] → [category|SW 3.1.9|Newly identified competence genes]
  • [category|SW 6|Groups of genes] → [category|SW 6.2|Membrane proteins]

    • Gene

    Coordinates
    1,530,537 → 1,531,865

    Phenotypes of a mutant

  • defects in sporulation and unable to grow on glucose as single carbon source [Pubmed|11976308]

    • The protein

    Catalyzed reaction/ biological activity

  • Acetyl-CoA enzyme N(6)-(dihydrolipoyl)lysine = CoA enzyme N(6)-(S-acetyldihydrolipoyl)lysine (according to Swiss-Prot)

    • Protein family

  • lipoyl-binding domain (according to Swiss-Prot)

    • Paralogous protein(s)

  • [protein|C4B6C3EE560C8BD353FEABB1A607C89C20DC8D34|AcoC], [protein|262C9FD20C7A70B6F1FEB57735FA800F38EAB25A|BkdB], [protein|02BA02D10DFB06E51101D8CF76BCF5BED94D7CA2|OdhB]

    • Kinetic information

  • Michaelis-Menten [Pubmed|6414463]

    • Modification

  • phosphorylated (Ser/Thr/Tyr) [Pubmed|17726680]

    • [SW|Cofactors]

  • lipoic acid

    • Effectors of protein activity

  • Inhibited by 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''), [PDB|2PDE] (peripheral subunit binding domain, ''Geobacillus stearothermophilus''), [PDB|1LAC] (lipoyl domain, ''Geobacillus stearothermophilus''), [PDB|1B5S] (catalytic domain (residues 184-425) , ''Geobacillus stearothermophilus'')

    • [SW|Localization]

  • membrane associated [Pubmed|18763711]
  • cytoplasm (homogeneously distributed throughout the cell) [Pubmed|24825009]

    • additional information

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

    • Expression and Regulation

    Operons

    genes
    [gene|953DE0F0B81894ECFF4C0693511AC238BF3D0C0A|pdhA]-[gene|458E967052D1093A0F48AE0E6B6CCA0F52EAC44D|pdhB]-[gene|2F40086E35FA32136B9A89C530A86D714FE9460C|pdhC]-[gene|E9BBAE86DF3E536A987179CC394B472F6F710498|pdhD]
    description
    [Pubmed|11976308]

    sigma factors

  • [protein|360F48D576DE950DF79C1A2677B7A35A8D8CC30C|SigA]: sigma factor, [Pubmed|20081037], in [regulon|360F48D576DE950DF79C1A2677B7A35A8D8CC30C|SigA regulon]

    • regulatory mechanism

  • [regulon|stringent response|stringent response]: negative regulation, due to presence of guanine at 1 position of the transcript [Pubmed|20081037], in [regulon|stringent response|stringent response]

    • regulation

  • ''[protein|search|pdhA]'': expression activated by glucose (1.9-fold) [Pubmed|12850135]
    • view in new tab

    genes
    [gene|2F40086E35FA32136B9A89C530A86D714FE9460C|pdhC]-[gene|E9BBAE86DF3E536A987179CC394B472F6F710498|pdhD]
    description
    [Pubmed|11976308]

    regulation

  • ''[protein|search|pdhA]'': expression activated by glucose (1.9-fold) [Pubmed|12850135]
    • view in new tab

    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

  • 19476487,9655937,2227213,6805383,1794583,24798336,27074917

    • Original publications

  • 9352926,24825009,9352926,17726680,12850135,18763711,6414463,11976308,20081037,22862776,15378759