A0A0D2XVZ1 · A0A0D2XVZ1_FUSOF
- ProteinDihydrolipoyl dehydrogenase
- Gene28949803
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids508 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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 | 91 | FAD (UniProtKB | ChEBI) | |||
Binding site | 155 | FAD (UniProtKB | ChEBI) | |||
Binding site | 184-186 | FAD (UniProtKB | ChEBI) | |||
Binding site | 221-228 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 244 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 314 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 355 | FAD (UniProtKB | ChEBI) | |||
Binding site | 361-364 | FAD (UniProtKB | ChEBI) | |||
Active site | 487 | Proton acceptor | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | glycine cleavage complex | |
Cellular Component | mitochondrial nucleoid | |
Cellular Component | oxoglutarate dehydrogenase complex | |
Cellular Component | pyruvate dehydrogenase complex | |
Molecular Function | dihydrolipoyl dehydrogenase activity | |
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | glycine dehydrogenase (decarboxylating) activity | |
Molecular Function | oxoglutarate dehydrogenase (succinyl-transferring) activity | |
Molecular Function | pyruvate dehydrogenase activity | |
Biological Process | 2-oxoglutarate metabolic process | |
Biological Process | glycine catabolic process | |
Biological Process | hydrogen peroxide metabolic process | |
Biological Process | isoleucine catabolic process | |
Biological Process | L-leucine catabolic process | |
Biological Process | L-serine biosynthetic process | |
Biological Process | pyruvate metabolic process | |
Biological Process | valine catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDihydrolipoyl dehydrogenase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Nectriaceae > Fusarium > Fusarium oxysporum species complex
Accessions
- Primary accessionA0A0D2XVZ1
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for disulfide bond.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Disulfide bond | 82↔87 | Redox-active | |||
Keywords
- PTM
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 44-370 | FAD/NAD(P)-binding | |||
Domain | 389-498 | 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
- Length508
- Mass (Da)54,265
- Last updated2015-04-29 v1
- Checksum3C4E4437A18178BA
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AFQF01002774 EMBL· GenBank· DDBJ | EGU78654.1 EMBL· GenBank· DDBJ | Genomic DNA |