SubtiBank SubtiBank
pdhD [Mon Jan 18 2016 15:28:49 GMT+0100 (CET)]
You are currently viewing an outdated version of SubtiWiki. Please use the newest version!

pdhD [Mon Jan 18 2016 15:28:49 GMT+0100 (CET)]

dihydrolipoamide dehydrogenase E3 subunit of both pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes
locus
BSU14610
pI
4.00
mw
49.00 kDa
function
links glycolysis and TCA cycle, enzyme in TCA cycle
product
dihydrolipoamide dehydrogenase E3 subunit
of both pyruvate dehydrogenase and 2-oxoglutarate
dehydrogenase complexes
essential
no
ec
1.8.1.4
synonyms
citL

Genomic Context

      

categories

  • [category|SW 2|Metabolism] → [category|SW 2.2|Carbon metabolism] → [category|SW 2.2.1|Carbon core metabolism] → [category|SW 2.2.1.4|TCA cycle]
  • [category|SW 6|Groups of genes] → [category|SW 6.4|Phosphoproteins] → [category|SW 6.4.8|Phosphorylation on either a Ser, Thr or Tyr residue]
  • [SW|Categories] containing this gene/protein

  • [SW|carbon core metabolism], [SW|most abundant proteins]
  • This gene is a member of the following [SW|regulons]

  • [SW|stringent response]
  • Gene

    Coordinates on the chromosome (coding sequence)
    1,531,870 -> 1,533,282

    Phenotypes of a mutant

  • defects in sporulation and unable to grow on glucose as single carbon source [Pubmed|11976308]
  • The protein

    Catalyzed reaction/ biological activity

  • Protein N(6)-(dihydrolipoyl)lysine NAD = protein N(6)-(lipoyl)lysine NADH (according to Swiss-Prot)
  • Protein family

  • class-I pyridine nucleotide-disulfide oxidoreductase family (according to Swiss-Prot)
  • Paralogous protein(s)

  • [protein|search|AcoL], [protein|search|LpdV]
  • Kinetic information

  • Michaelis-Menten [Pubmed|6414463]
  • Modification

  • phosphorylated (Ser/Thr/Tyr) [Pubmed|17726680]
  • Effectors of protein activity

  • Inhibited thiamine 2-thiothiazolone diphosphate and NADH [Pubmed|6414463]
  • Low sensibility to NADPH [Pubmed|6414463]
  • Structure

  • [PDB|1EBD] (complex with binding domain of dihydrolipoamide acetylase, Geobacillus stearothermophilus), [PDB|1EBD] (complex with binding domain of dihydrolipoamide acetylase, ''Geobacillus stearothermophilus'')
  • [SW|Localization]

  • cytoplasm (according to Swiss-Prot)
  • [SW|Interactions]

  • [protein|search|OdhA]-[protein|search|OdhB]-[protein|search|PdhD] [Pubmed|20933603]
  • [protein|search|PdhA]-[protein|search|PdhB]-[protein|search|PdhC]-[protein|search|PdhD]
  • Expression and Regulation

    [SW|Sigma factor]

  • ''[protein|search|pdhA]'': [protein|search|SigA] [Pubmed|20081037]
  • ''[protein|search|pdhC]'': [protein|search|SigA] [Pubmed|11976308]
  • Regulation

  • ''[protein|search|pdhA]'': expression activated by glucose (2.0-fold) [Pubmed|12850135]
  • subject to negative stringent control upon amino acid limitation [Pubmed|20081037]
  • Regulatory mechanism

  • stringent response: due to presence of guanine at 1 position of the transcript [Pubmed|20081037]
  • Additional information

  • belongs to the 100 [[most abundant proteins]] [PubMed|15378759]
  • Biological materials

    lacZ fusion

  • pGP723 (in [protein|search|pAC5]), available in [SW|Stülke] lab
  • two-hybrid system

  • ''B. pertussis'' adenylate cyclase-based bacterial two hybrid system ([SW|BACTH]), available in [SW|Stülke] lab
  • FLAG-tag construct

  • GP1427 (spc, based on [SW|pGP1331]), available in the [SW|Stülke] lab
  • Antibody

  • **
  • References

    Reviews

  • 19476487,9655937,2227213,6805383,10672230,24798336
  • Original publications

  • 12850135,6414463,11976308,17726680,20081037,20933603,24204596,15378759