Difference between revisions of "PdhC"

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(References)
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* '''Sigma factor:'''  
 
* '''Sigma factor:'''  
** ''[[pdhA]]'': [[SigA]] {{PubMed|11976308}}
+
** ''[[pdhA]]'': [[SigA]] {{PubMed|20081037}}
 
** ''[[pdhC]]'': [[SigA]] {{PubMed|11976308}}
 
** ''[[pdhC]]'': [[SigA]] {{PubMed|11976308}}
  
* '''Regulation:''' expression activated by glucose (1.9 fold) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed]
+
* '''Regulation:'''  
 +
** ''[[pdhA]]'': expression activated by glucose (1.9-fold) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed]
 +
** subject to negative stringent control upon amino acid limitation {{PubMed|20081037}}
  
 
* '''Regulatory mechanism:'''  
 
* '''Regulatory mechanism:'''  
 
+
** stringent response: due to presence of guanine at +1 position of the transcript {{PubMed|20081037}}
* '''Additional information:'''
 
  
 
=Biological materials =
 
=Biological materials =
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=References=
 
=References=
  
<pubmed>9352926,,9352926,17726680 ,12850135 18763711 6414463 11976308</pubmed>
+
<pubmed>9352926,,9352926,17726680 ,12850135 18763711 6414463 11976308 20081037 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 18:53, 19 January 2010

  • Description: pyruvate dehydrogenase (dihydrolipoamide acetyltransferase E2 subunit)

Gene name pdhC
Synonyms
Essential no
Product pyruvate dehydrogenase
(dihydrolipoamide acetyltransferase E2 subunit)
Function links glycolysis and TCA cycle
Metabolic function and regulation of this protein in SubtiPathways:
Central C-metabolism
MW, pI 47 kDa, 4.855
Gene length, protein length 1326 bp, 442 aa
Immediate neighbours pdhB, pdhD
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
PdhC context.gif
This image was kindly provided by SubtiList







The gene

Basic information

  • Locus tag: BSU14600

Phenotypes of a mutant

  • defects in sporulation and unable to grow on glucose as single carbon source PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine (according to Swiss-Prot)
  • Protein family: lipoyl-binding domain (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

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

Database entries

  • Structure: 1W88 (E1 in complex with subunit binding domain of E2, Geobacillus stearothermophilus), 2PDE (peripheral subunit binding domain, Geobacillus stearothermophilus), 1LAC (lipoyl domain, Geobacillus stearothermophilus), 1B5S (catalytic domain (residues 184-425) , Geobacillus stearothermophilus)
  • UniProt: P21883
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • pdhA: expression activated by glucose (1.9-fold) 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

Biological materials

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

Labs working on this gene/protein

Arthur Aronson, Purdue University, West Lafayette, USA homepage

Your additional remarks

References