pdhD
168
dihydrolipoamide dehydrogenase E3 subunit of both pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes
Locus
BSU_14610
Molecular weight
49.57 kDa
Isoelectric point
4.76
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
E.C.
1.8.1.4
Synonyms
pdhD, citL
Outlinks
Genomic Context
Categories containing this gene/protein
List of homologs in different organisms, belongs to COG1249 (Galperin et al., 2021)
This gene is a member of the following regulons
Gene
Coordinates
1,531,870 1,533,282
Phenotypes of a mutant
defects in sporulation and unable to grow on glucose as single carbon source PubMed
The protein
Catalyzed reaction/ biological activity
Protein N6-(dihydrolipoyl)lysine + NAD+ --> protein N6-(lipoyl)lysine + NADH2 (according to UniProt)
Protein family
FAD (according to UniProt)
Structure
1EBD (PDB) (complex with binding domain of dihydrolipoamide acetylase, Geobacillus stearothermophilus), 1EBD (PDB) (complex with binding domain of dihydrolipoamide acetylase, Geobacillus stearothermophilus)
Modification
phosphorylated (Ser/Thr/Tyr) PubMed
Effectors of protein activity
Kinetic information
Michaelis-Menten PubMed
Paralogous protein(s)
cytoplasm (according to UniProt)
Additional information
belongs to the 100 most abundant proteins PubMed
Expression and Regulation
Operons
Description
Regulation
Regulatory mechanism
stringent response: negative regulation, due to presence of guanine at 1 position of the transcript PubMed, in stringent response
Sigma factors
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Biological materials
Mutant
Two-hybrid system
FLAG-tag construct
LacZ fusion
References
Reviews
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Original Publications
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Time of last update: 2025-04-06 01:34:13
Author of last update: Jstuelk