A0A0K3AS75 · A0A0K3AS75_BABMR
- ProteinDihydrolipoyl dehydrogenase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids473 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
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 | 60 | FAD (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 124 | FAD (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 152-154 | FAD (UniProtKB | ChEBI) | ||||
Sequence: TGS | ||||||
Binding site | 188-195 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GAGAIGLE | ||||||
Binding site | 211 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 278 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 319 | FAD (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 325-328 | FAD (UniProtKB | ChEBI) | ||||
Sequence: MLAH | ||||||
Active site | 452 | Proton acceptor | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrion | |
Cellular Component | oxoglutarate dehydrogenase complex | |
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
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Piroplasmida > Babesiidae > Babesia
Accessions
- Primary accessionA0A0K3AS75
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Disulfide bond | 51↔56 | Redox-active | ||||
Sequence: CLNVGC |
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 14-334 | FAD/NAD(P)-binding | ||||
Sequence: DLAVIGGGPGGYVAAIKAAQEGLNVACIEHRGSLGGTCLNVGCIPSKLLINTAYNYHFISHGLAGTGLSVSGVSYKFGDIVAAKDKCVKSLIQGIEFLFKKNKVQYIKGWGTIKSPTQIQVTTSAGTDILEAKNIIIATGSIPSPFPPLPFSDKVVSSDQVLSLPTCPKSMIIVGAGAIGLEMASVFNWLGTKVKVLEFSKKICSVMDHEISDALKTALVKQGIEIHTDTKVNGGTESSTGVKVTADKNGEYVDHEVELVLVATGRIPYTENLGLEAIGVETIRGKVPVTSNLSLEKYPNIYAIGDVIDGPMLAHKAEDDG | ||||||
Domain | 354-462 | Pyridine nucleotide-disulphide oxidoreductase dimerisation | ||||
Sequence: VPSVIYTHPEVSGVGQTEQSLIESGIKYTKGVFPLVANSRAKLANETTGFVKVLSDEESGKILGAWIFGTQASELIATFGLAITYGASAQDVSRVCFAHPTVSEAIKEA |
Sequence similarities
Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length473
- Mass (Da)50,136
- Last updated2015-11-11 v1
- Checksum1F89905F8C2FCEDA
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LN871598 EMBL· GenBank· DDBJ | CTQ41453.1 EMBL· GenBank· DDBJ | Genomic DNA |