Q8NTE1 · DLDH_CORGL
- ProteinDihydrolipoyl dehydrogenase
- Genelpd
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids469 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Lipoamide dehydrogenase is an essential component of the pyruvate dehydrogenase (PDH) and 2-oxoglutarate dehydrogenase (ODH) complexes. Catalyzes the reoxidation of dihydrolipoyl groups which are covalently attached to the lipoate acyltransferase components (E2) of the complexes. Also catalyzes a reversible NADH:NAD+ transhydrogenation, and is able to transfer electrons from NADH to various redox-active compounds and quinones. May be involved in quinone redox cycling in C.glutamicum.
Miscellaneous
The active site is a redox-active disulfide bond.
Overexpression of LPD enhances sensitivity to menadione, but has no effect on sensitivity to paraquat or hydrogen peroxide.
Catalytic activity
- N6-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD+ = H+ + N6-[(R)-lipoyl]-L-lysyl-[protein] + NADH
Cofactor
Note: Binds 1 FAD per subunit.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.636 μM | lipoate |
pH Dependence
Optimum pH is 7.0-7.5 for the reduction of lipoate by NADH.
Temperature Dependence
Optimum temperature is 50 degrees Celsius for the reduction of lipoate by NADH.
Pathway
Carbohydrate metabolism; tricarboxylic acid cycle; succinyl-CoA from 2-oxoglutarate (dehydrogenase route): step 1/1.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 34-42 | FAD (UniProtKB | ChEBI) | ||||
Sequence: EKQYWGGVC | ||||||
Binding site | 51 | FAD (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 114 | FAD (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 179-183 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GAGAI | ||||||
Binding site | 202 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 269-272 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: SVGF | ||||||
Binding site | 312 | FAD (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 320 | FAD (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Active site | 448 | Proton acceptor | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | dihydrolipoyl dehydrogenase activity | |
Molecular Function | flavin adenine dinucleotide binding | |
Biological Process | tricarboxylic acid cycle |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDihydrolipoyl dehydrogenase
- EC number
- Short namesLPD
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Corynebacteriaceae > Corynebacterium
Accessions
- Primary accessionQ8NTE1
- Secondary accessions
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for initiator methionine, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000420523 | 2-469 | Dihydrolipoyl dehydrogenase | |||
Sequence: TEHYDVVVLGAGPGGYVSAIRAAQLGKKVAVIEKQYWGGVCLNVGCIPSKSLIKNAEVAHTFTHEKKTFGINGEVTFNYEDAHKRSRGVSDKIVGGVHYLMKKNKIIEIHGLGNFKDAKTLEVTDGKDAGKTITFDDCIIATGSVVNTLRGVDFSENVVSFEEQILNPVAPKKMVIVGAGAIGMEFAYVLGNYGVDVTVIEFMDRVLPNEDAEVSKVIAKAYKKMGVKLLPGHATTAVRDNGDFVEVDYQKKGSDKTETLTVDRVMVSVGFRPRVEGFGLENTGVKLTERGAIEIDDYMRTNVDGIYAIGDVTAKLQLAHVAEAQGIVAAETIAGAETQTLGDYMMMPRATFCNPQVSSFGYTEEQAKEKWPDREIKVASFPFSANGKAVGLAETDGFAKIVADAEFGELLGAHLVGANASELINELVLAQNWDLTTEEISRSVHIHPTLSEAVKEAAHGISGHMINF | ||||||
Disulfide bond | 42↔47 | Redox-active | ||||
Sequence: CLNVGC |
Keywords
- PTM
Interaction
Subunit
Homodimer (By similarity).
Part of an unusual ODH/PDH supercomplex, consisting of AceE (E1), AceF (E2), and Lpd (E3) together with OdhA (E1+E2)
Part of an unusual ODH/PDH supercomplex, consisting of AceE (E1), AceF (E2), and Lpd (E3) together with OdhA (E1+E2)
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length469
- Mass (Da)50,652
- Last updated2002-10-01 v1
- Checksum7F8FFE6B510B8725
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 382 | in Ref. 1; CAA76340 | ||||
Sequence: F → L |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Y16642 EMBL· GenBank· DDBJ | CAA76340.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BA000036 EMBL· GenBank· DDBJ | BAB97759.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BX927149 EMBL· GenBank· DDBJ | CAF19080.1 EMBL· GenBank· DDBJ | Genomic DNA |