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

Original publications

Leigh G Monahan, Isabella V Hajduk, Sinead P Blaber, Ian G Charles, Elizabeth J Harry
Coordinating bacterial cell division with nutrient availability: a role for glycolysis.
mBio: 2014, 5(3);e00935-14
[PubMed:24825009] [WorldCat.org] [DOI] (I e)

Irnov Irnov, Cynthia M Sharma, Jörg Vogel, Wade C Winkler
Identification of regulatory RNAs in Bacillus subtilis.
Nucleic Acids Res: 2010, 38(19);6637-51
[PubMed:20525796] [WorldCat.org] [DOI] (I p)

Shigeo Tojo, Kanako Kumamoto, Kazutake Hirooka, Yasutaro Fujita
Heavy involvement of stringent transcription control depending on the adenine or guanine species of the transcription initiation site in glucose and pyruvate metabolism in Bacillus subtilis.
J Bacteriol: 2010, 192(6);1573-85
[PubMed:20081037] [WorldCat.org] [DOI] (I p)

Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759] [WorldCat.org] [DOI] (P p)

Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135] [WorldCat.org] [DOI] (P p)

Haichun Gao, Xin Jiang, Kit Pogliano, Arthur I Aronson
The E1beta and E2 subunits of the Bacillus subtilis pyruvate dehydrogenase complex are involved in regulation of sporulation.
J Bacteriol: 2002, 184(10);2780-8
[PubMed:11976308] [WorldCat.org] [DOI] (P p)

M M Nakano, Y P Dailly, P Zuber, D P Clark
Characterization of anaerobic fermentative growth of Bacillus subtilis: identification of fermentation end products and genes required for growth.
J Bacteriol: 1997, 179(21);6749-55
[PubMed:9352926] [WorldCat.org] [DOI] (P p)

P N Lowe, J A Hodgson, R N Perham
Dual role of a single multienzyme complex in the oxidative decarboxylation of pyruvate and branched-chain 2-oxo acids in Bacillus subtilis.
Biochem J: 1983, 215(1);133-40
[PubMed:6414463] [WorldCat.org] [DOI] (P p)