pdhC

pdhC
168

pyruvate dehydrogenase (dihydrolipoamide acetyltransferase E2 subunit)

Locus
BSU_14600
Molecular weight
47.38 kDa
Isoelectric point
4.86
Protein length
442 aaSequenceBlast
Gene length
1329 bpSequenceBlast
Function
links glycolysis and TCA cycle
Product
pyruvate dehydrogenase (dihydrolipoamide acetyltransferase E2 subunit)
Essential
no
E.C.
2.3.1.12
Synonyms
pdhC
Outlinks
BsubCyc SubtiList UniProt STRING Genoscapist PaperBLAST

Genomic Context

Categories containing this gene/protein

List of homologs in different organisms, belongs to COG0508 (Galperin et al., 2021)

This gene is a member of the following regulons

Gene
Coordinates
1,530,537 1,531,865
Phenotypes of a mutant
the mutant tends to acquire suppressor mutations that result in improved growth PubMed
defects in sporulation and unable to grow on glucose as single carbon source PubMed
poor growth PubMed
non-transformable PubMed
The protein
Catalyzed reaction/ biological activity
(R)-N6-dihydrolipoyl-L-lysyl-[protein] + acetyl-CoA --> (R)-N6-(S8-acetyldihydrolipoyl)-L-lysyl-[protein] + CoA (according to UniProt)
Protein family
2-oxoacid dehydrogenase family (according to UniProt)
Domains
Lipoyl-binding domain (aa 2-77) (according to UniProt)
Peripheral subunit-binding domain (PSBD) (aa 141-178) (according to UniProt)
Cofactors
lipoic acid (on Lys-43), can probably be removed by SrtN PubMed
Structure
1W88 (PDB) (E1 in complex with subunit binding domain of E2, Geobacillus stearothermophilus) PubMed
2PDE (PDB) (peripheral subunit binding domain, Geobacillus stearothermophilus)
1LAC (PDB) (lipoyl domain, Geobacillus stearothermophilus)
1B5S (PDB) (catalytic domain (residues 184-425) , Geobacillus stearothermophilus)
P21883 (AlphaFold)
Modification
phosphorylated (Ser/Thr/Tyr) PubMed
Effectors of protein activity
Inhibited by thiamine 2-thiothiazolone diphosphate and NADH PubMed
Low sensibility to NADPH
Kinetic information
Michaelis-Menten PubMed
Paralogous protein(s)
AcoC, OdhB, BkdB
Localization
membrane associated PubMed
cytoplasm (homogeneously distributed throughout the cell) PubMed
Additional information
belongs to the 100 most abundant proteins PubMed
Expression and Regulation
Operons
Genes
pdhA-pdhB-pdhC-pdhD
Description
PubMed
Regulation
''pdhA'': expression activated by glucose (1.9-fold) PubMed
Regulatory mechanism
stringent response: negative regulation, due to presence of guanine at 1 position of the transcript PubMed, in stringent response
Sigma factors
SigA: sigma factor, PubMed, in sigA regulon
Open in new tab

pdhA→pdhD

2025-03-29 04:16:44

ghost

117

797fea7dcbe4317f63eb94d44165272d12ff3ae4

3D5EA61F84C1F6538A394D4F9A00FD4029ED115F

Genes
pdhC-pdhD
Description
PubMed
Regulation
''pdhA'': expression activated by glucose (1.9-fold) PubMed
Open in new tab

pdhC→pdhD

2025-04-04 07:59:38

ghost

108

22b57c718f31ad11fe44c3a9b66c0348a0c6dcab

F1C43D78FC4D596937F2D6B16CB47827D858EE6D

Biological materials
Mutant
BKE14600 (pdhC::erm trpC2) available at BGSC, PubMed, upstream reverse: _UP1_CACAGTTCTCGACCTCCTAG, downstream forward: _UP4_TTAATTTTAATGGAGGCGTA
BKK14600 (pdhC::kan trpC2) available at BGSC, PubMed, upstream reverse: _UP1_CACAGTTCTCGACCTCCTAG, downstream forward: _UP4_TTAATTTTAATGGAGGCGTA
Labs working on this gene/protein
Arthur Aronson, Purdue University, West Lafayette, USA homepage
References
Reviews
Loading
Original Publications
Loading

2F40086E35FA32136B9A89C530A86D714FE9460C

Page visits: 5507

Time of last update: 2025-04-06 02:17:45

Author of last update: Jstuelk