O84561 · DLDH_CHLTR
- ProteinDihydrolipoyl dehydrogenase
- GenelpdA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids465 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2. It contains multiple copies of 3 enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
Miscellaneous
The active site is a redox-active disulfide bond.
Catalytic activity
- N6-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD+ = N6-[(R)-lipoyl]-L-lysyl-[protein] + NADH + H+
Cofactor
Note: Binds 1 FAD per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 34-42 | FAD (UniProtKB | ChEBI) | ||||
Sequence: EKREAGGTC | ||||||
Binding site | 51 | FAD (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 114 | FAD (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 180-184 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GGGVI | ||||||
Binding site | 203 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 237 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 264-267 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: SIGR | ||||||
Binding site | 307 | FAD (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 315 | FAD (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Active site | 439 | Proton acceptor | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | dihydrolipoyl dehydrogenase activity | |
Molecular Function | flavin adenine dinucleotide binding |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDihydrolipoyl dehydrogenase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Chlamydiota > Chlamydiia > Chlamydiales > Chlamydiaceae > Chlamydia/Chlamydophila group > Chlamydia
Accessions
- Primary accessionO84561
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000068026 | 1-465 | Dihydrolipoyl dehydrogenase | |||
Sequence: MNEAFDCVVIGAGPGGYVAAITAAQAGLKTALIEKREAGGTCLNRGCIPSKALLAGAEVVTQIRHADQFGIHVEGFSINYPAMVQRKDSVVRSIRDGLNGLIRSNKITVFSGRGSLISSTEVKILGENPSVIKAHSIILATGSEPRAFPGIPFSAESPRILCSTGVLNLKEIPQKMAIIGGGVIGCEFASLFHTLGSEVSVIEASSQILALNNPDISKTMFDKFTRQGLRFVLEASVSNIEDIGDRVRLTINGNVEEYDYVLVSIGRRLNTENIGLDKAGVICDERGVIPTDATMRTNVPNIYAIGDITGKWQLAHVASHQGIIAARNIAGHKEEIDYSAVPSVIFTFPEVASVGLSPTAAQQQKIPVKVTKFPFRAIGKAVAMGEADGFAAIISHETTQQILGAYVIGPHASSLISEITLAVRNELTLPCIYETIHAHPTLAEVWAESALLAVDTPLHMPPAKK | ||||||
Disulfide bond | 42↔47 | Redox-active | ||||
Sequence: CLNRGC |
Keywords
- PTM
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length465
- Mass (Da)49,491
- Last updated1998-11-01 v1
- Checksum56449CCD2AB61477
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE001273 EMBL· GenBank· DDBJ | AAC68159.1 EMBL· GenBank· DDBJ | Genomic DNA |