Q8I5A0 · Q8I5A0_PLAF7
- ProteinDihydrolipoyl dehydrogenase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids512 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
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 | 72 | FAD (UniProtKB | ChEBI) | |||
Binding site | 136 | FAD (UniProtKB | ChEBI) | |||
Binding site | 164-166 | FAD (UniProtKB | ChEBI) | |||
Binding site | 218-225 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 241 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 310 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 352 | FAD (UniProtKB | ChEBI) | |||
Binding site | 358-361 | FAD (UniProtKB | ChEBI) | |||
Active site | 491 | Proton acceptor | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial matrix | |
Cellular Component | mitochondrion | |
Cellular Component | oxoglutarate dehydrogenase complex | |
Molecular Function | catalytic activity | |
Molecular Function | dihydrolipoyl dehydrogenase activity | |
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | protein homodimerization activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDihydrolipoyl dehydrogenase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Haemosporida > Plasmodiidae > Plasmodium > Plasmodium (Laverania)
Accessions
- Primary accessionQ8I5A0
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 25-367 | FAD/NAD(P)-binding | |||
Domain | 393-501 | Pyridine nucleotide-disulphide oxidoreductase dimerisation | |||
Sequence similarities
Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length512
- Mass (Da)57,228
- Last updated2009-09-22 v2
- Checksum50F2FC7739E34E4A
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LN999947 EMBL· GenBank· DDBJ | CZT99481.1 EMBL· GenBank· DDBJ | Genomic DNA |