Difference between revisions of "PdhA"

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m (Reverted edits by 134.76.70.252 (talk) to last revision by Jstuelk)
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* '''Operon:''' ''[[pdhA]]-[[pdhB]]-[[pdhC]]-[[pdhD]]'' {{PubMed|11976308}}
 
* '''Operon:''' ''[[pdhA]]-[[pdhB]]-[[pdhC]]-[[pdhD]]'' {{PubMed|11976308}}
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=pdhA_1528326_1529441_1 pdhA] {{PubMed|22383849}}
  
 
* '''Sigma factor:''' [[SigA]] {{PubMed|20081037}}
 
* '''Sigma factor:''' [[SigA]] {{PubMed|20081037}}

Revision as of 08:08, 13 April 2012

  • 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
Interactions involving this protein in SubtInteract: PdhA
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







Categories containing this gene/protein

carbon core metabolism, essential genes

This gene is a member of the following regulons

stringent response

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

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 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

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

Reviews

Original publications