Difference between revisions of "PdhD"

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* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1EBD 1EBD] (complex with binding domain of dihydrolipoamide acetylase, Geobacillus stearothermophilus),  [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1EBD 1EBD] (complex with binding domain of dihydrolipoamide acetylase, ''Geobacillus stearothermophilus'')
 
* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1EBD 1EBD] (complex with binding domain of dihydrolipoamide acetylase, Geobacillus stearothermophilus),  [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1EBD 1EBD] (complex with binding domain of dihydrolipoamide acetylase, ''Geobacillus stearothermophilus'')
  
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P21880 P21880]
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* '''UniProt:''' [http://www.uniprot.org/uniprot/P21880 P21880]
  
 
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU14610]
 
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU14610]
  
* '''E.C. number:''' [http://www.expasy.org/enzyme/1.8.1.4 1.8.1.4]  
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* '''E.C. number:''' [http://www.expasy.org/enzyme/1.8.1.4 1.8.1.4]
  
 
=== Additional information===
 
=== Additional information===

Revision as of 12:35, 20 July 2009

  • 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
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
PdhD context.gif
This image was kindly provided by SubtiList







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]

Additional information

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
  • 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)
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation: expression activated by glucose (2.0 fold) PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

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)

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)