PdhD

• Description: dihydrolipoamide dehydrogenase E3 subunit of both pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes
  
  

Gene name	pdhD
Synonyms	citL
Essential	no
Product	dihydrolipoamide dehydrogenase E3 subunit of both pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes
Function	links glycolysis and TCA cycle, enzyme in TCA cycle
Interactions involving this protein in SubtInteract: PdhD
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism
MW, pI	49 kDa, 4.76
Gene length, protein length	1410 bp, 470 aa
Immediate neighbours	pdhC, slp
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

carbon core metabolism

This gene is a member of the following regulons

stringent response

The gene

Basic information

• Locus tag: BSU14610

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]

The protein

Basic information/ Evolution

• 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):

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 PubMed

• Interactions:
  • OdhA-OdhB-PdhD PubMed
  • PdhA-PdhB-PdhC-PdhD

• Localization: cytoplasm (according to Swiss-Prot)

Database entries

• Structure: 1EBD (complex with binding domain of dihydrolipoamide acetylase, Geobacillus stearothermophilus), 1EBD (complex with binding domain of dihydrolipoamide acetylase, Geobacillus stearothermophilus)

• UniProt: P21880

• KEGG entry: [3]

• E.C. number: 1.8.1.4

Expression and regulation

• • pdhA-pdhB-pdhC-pdhD PubMed
  • pdhC-pdhD PubMed

• Expression browser: pdhD PubMed

• Sigma factor:
  • pdhA: SigA PubMed
  • pdhC: SigA PubMed

• Regulation:
  • pdhA: expression activated by glucose (2.0-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

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion: pGP723 (in pAC5), available in Stülke lab

• GFP fusion:

• two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab

• Antibody:

References

Reviews

Kai Tittmann
Reaction mechanisms of thiamin diphosphate enzymes: redox reactions.
FEBS J: 2009, 276(9);2454-68
[PubMed:19476487] [WorldCat.org] [DOI] (I p)

K F Sheu, J P Blass
The alpha-ketoglutarate dehydrogenase complex.
Ann N Y Acad Sci: 1999, 893;61-78
[PubMed:10672230] [WorldCat.org] [DOI] (P p)

U Neveling, S Bringer-Meyer, H Sahm
Gene and subunit organization of bacterial pyruvate dehydrogenase complexes.
Biochim Biophys Acta: 1998, 1385(2);367-72
[PubMed:9655937] [WorldCat.org] [DOI] (P p)

M S Patel, T E Roche
Molecular biology and biochemistry of pyruvate dehydrogenase complexes.
FASEB J: 1990, 4(14);3224-33
[PubMed:2227213] [WorldCat.org] [DOI] (P p)

P A Frey
Mechanism of coupled electron and group transfer in Escherichia coli pyruvate dehydrogenase.
Ann N Y Acad Sci: 1982, 378;250-64
[PubMed:6805383] [WorldCat.org] [DOI] (P p)