Difference between revisions of "PdhA"

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(Biological materials)
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* '''Operon:''' ''[[pdhA]]-[[pdhB]]-[[pdhC]]-[[pdhD]]'' {{PubMed|11976308}}
 
* '''Operon:''' ''[[pdhA]]-[[pdhB]]-[[pdhC]]-[[pdhD]]'' {{PubMed|11976308}}
  
* '''Sigma factor:''' [[SigA]] {{PubMed|11976308}}
+
* '''Sigma factor:''' [[SigA]] {{PubMed|20081037}}
  
* '''Regulation:''' expression activated by glucose (3.4) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed]
+
* '''Regulation:'''  
 +
** expression activated by glucose (3.4) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed]
 +
** subject to negative stringent control upon amino acid limitation (due to control of'' [[ptsG]]'' transcription initiation) {{PubMed|20081037}}
  
 
* '''Regulatory mechanism:'''  
 
* '''Regulatory mechanism:'''  
 +
** stringent response: due to presence of guanine at +1 position of the transcript {{PubMed|20081037}}
  
 
* '''Additional information:'''
 
* '''Additional information:'''
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=References=
 
=References=
  
<pubmed>9352926,,12850135 6414463 11976308</pubmed>
+
<pubmed>9352926,,12850135 6414463 11976308 20081037 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 18:49, 19 January 2010

  • Description: pyruvate dehydrogenase (E1 alpha subunit)

Gene name pdhA
Synonyms aceA
Essential yes
Product pyruvate dehydrogenase (E1 alpha subunit)
Function links glycolysis and TCA cycle
Metabolic function and regulation of this protein in SubtiPathways:
Central C-metabolism
MW, pI 41 kDa, 5.837
Gene length, protein length 1113 bp, 371 aa
Immediate neighbours ykyA, pdhB
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
PdhA context.gif
This image was kindly provided by SubtiList







The gene

Basic information

  • Locus tag: BSU14580

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

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):

Extended information on the protein

  • Kinetic information: Michaelis-Menten PubMed
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
    • Inhibited thiamine 2-thiothiazolone diphosphate and NADH PubMed
    • Low sensibility to NADPH
  • Localization:

Database entries

  • Structure: 1W88 (E1 in complex with subunit binding domain of E2, Geobacillus stearothermophilus)
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • expression activated by glucose (3.4) PubMed
    • subject to negative stringent control upon amino acid limitation (due to control of ptsG transcription initiation) PubMed
  • Regulatory mechanism:
    • stringent response: due to presence of guanine at +1 position of the transcript PubMed
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Arthur Aronson, Purdue University, West Lafayette, USA homepage

Your additional remarks

References

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)

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)