pdhC

pyruvate dehydrogenase (dihydrolipoamide acetyltransferase E2 subunit)

locus: BSU_14600

pI: 4.86

mw: 47.38 kDa

protein length: 442 aa

gene length: 1329 bp

function: links glycolysis and TCA cycle

product: pyruvate dehydrogenase (dihydrolipoamide acetyltransferase E2 subunit)

essential: no

ec: 2.3.1.12

synonyms

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]
• poor growth [pubmed|28189581]
• non-transformable [pubmed|28189581]

The protein

Catalyzed reaction/ biological activity

• (R)-N⁶-dihydrolipoyl-L-lysyl-[protein] + acetyl-CoA --> (R)-N⁶-(S⁸-acetyldihydrolipoyl)-L-lysyl-[protein] + CoA (according to UniProt)

Protein family

• [SW|2-oxoacid dehydrogenase family] (according to UniProt)

Paralogous protein(s)

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

Kinetic information

• Michaelis-Menten [Pubmed|6414463]

[SW|Domains]

• [SW|Lipoyl-binding domain] (aa 2-77) (according to UniProt)
• [SW|Peripheral subunit-binding domain] (PSBD) (aa 141-178) (according to UniProt)

Modification

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

[SW|Cofactors]

• lipoic acid (on Lys-43), can probably be removed by [protein|A0A6CB19191A251BB5600C18E039978A9A34933C|SrtN] [pubmed|28900027]

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]

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

  regulation

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

Biological materials

Mutant

• BKE14600 ([gene|2F40086E35FA32136B9A89C530A86D714FE9460C|pdhC]::erm trpC2) available at [http://www.bgsc.org/getdetail.php?bgscid=BKE14600 BGSC], [Pubmed|28189581], upstream reverse: _UP1_CACAGTTCTCGACCTCCTAG, downstream forward: _UP4_TTAATTTTAATGGAGGCGTA
• BKK14600 ([gene|2F40086E35FA32136B9A89C530A86D714FE9460C|pdhC]::kan trpC2) available at [http://www.bgsc.org/getdetail.php?bgscid=BKK14600 BGSC], [Pubmed|28189581], upstream reverse: _UP1_CACAGTTCTCGACCTCCTAG, downstream forward: _UP4_TTAATTTTAATGGAGGCGTA

labs

• [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

• 9352926,24825009,9352926,17726680,12850135,18763711,6414463,11976308,20081037,22862776,15378759,28900027,28189581,31066113