PdhA

• Description: pyruvate dehydrogenase (E1 alpha subunit), required for Z-ring assembly in a pyruvate-dependent manner
  
  

Gene name	pdhA
Synonyms	aceA
Essential	yes PubMed, no PubMed
Product	pyruvate dehydrogenase (E1 alpha subunit)
Function	links glycolysis and TCA cycle
Gene expression levels in SubtiExpress: pdhA
Interactions involving this protein in SubtInteract: PdhA
Metabolic function and regulation of this protein in SubtiPathways: pdhA
MW, pI	41 kDa, 5.837
Gene length, protein length	1113 bp, 371 aa
Immediate neighbours	ykyA, pdhB
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

carbon core metabolism, essential genes, most abundant proteins

This gene is a member of the following regulons

stringent response

The gene

Basic information

• Locus tag: BSU14580

Phenotypes of a mutant

• pdhA is essential according to Kobayashi et al. 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

Database entries

• BsubCyc: BSU14580

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO₂ (according to Swiss-Prot)

• Protein family:

• Paralogous protein(s): AcoA, BkdAA

Extended information on the protein

• Kinetic information: Michaelis-Menten PubMed

• Domains:

• Modification:

• Cofactors:
  • thiamine pyrophosphate

• Effectors of protein activity:
  • Inhibited thiamine 2-thiothiazolone diphosphate and NADH PubMed
  • Low sensibility to NADPH

• Interactions:
  • PdhA-PdhB-PdhC-PdhD

• Localization:
  • colocalizes with the nucleoid (depending on the availability of pyruvate) PubMed

Database entries

• BsubCyc: BSU14580

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

• UniProt: P21881

• KEGG entry: [3]

• E.C. number: 1.2.4.1

Expression and regulation

• Operon: pdhA-pdhB-pdhC-pdhD PubMed

• Expression browser: pdhA PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • expression activated by glucose (3.4) PubMed
  • subject to negative stringent control upon amino acid limitation PubMed

• Regulatory mechanism:
  • stringent response: due to presence of guanine at +1 position of the transcript PubMed

• Additional information:
  • The mRNA has a long 5' leader region. This may indicate RNA-based regulation PubMed
  • belongs to the 100 most abundant proteins PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 5117 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 18311 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 4425 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 5452 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 7055 PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion: pGP721 (in pAC5), available in Stülke lab, pGP186 (in pAC7), available in Stülke lab

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

Arthur Aronson, Purdue University, West Lafayette, USA homepage

References

Reviews

Mulchand S Patel, Natalia S Nemeria, William Furey, Frank Jordan
The pyruvate dehydrogenase complexes: structure-based function and regulation.
J Biol Chem: 2014, 289(24);16615-23
[PubMed:24798336] [WorldCat.org] [DOI] (I p)

Kai Tittmann
Reaction mechanisms of thiamin diphosphate enzymes: redox reactions.
FEBS J: 2009, 276(9);2454-68
[PubMed:19476487] [WorldCat.org] [DOI] (I p)

U Neveling, S Bringer-Meyer, H Sahm
Gene and subunit organization of bacterial pyruvate dehydrogenase complexes.
Biochim Biophys Acta: 1998, 1385(2);367-72
[PubMed:9655937] [WorldCat.org] [DOI] (P p)

M S Patel, T E Roche
Molecular biology and biochemistry of pyruvate dehydrogenase complexes.
FASEB J: 1990, 4(14);3224-33
[PubMed:2227213] [WorldCat.org] [DOI] (P p)

P A Frey
Mechanism of coupled electron and group transfer in Escherichia coli pyruvate dehydrogenase.
Ann N Y Acad Sci: 1982, 378;250-64
[PubMed:6805383] [WorldCat.org] [DOI] (P p)