A0A8T9MVF1 · A0A8T9MVF1_9NEIS
- ProteinDihydrolipoyl dehydrogenase
- GenelpdA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids598 (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
Protein has several cofactor binding sites:
Note: Binds 1 FAD per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 164 | FAD (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 227 | FAD (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 306-313 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GGGIIGLE | ||||||
Binding site | 329 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 397 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 438 | FAD (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 444-447 | FAD (UniProtKB | ChEBI) | ||||
Sequence: MLAH | ||||||
Active site | 570 | Proton acceptor | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
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 lineageBacteria > Pseudomonadota > Betaproteobacteria > Neisseriales > Neisseriaceae > Conchiformibius
Accessions
- Primary accessionA0A8T9MVF1
Proteomes
PTM/Processing
Features
Showing features for disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Disulfide bond | 155↔160 | Redox-active | ||||
Sequence: CLNVGC |
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 3-77 | Lipoyl-binding | ||||
Sequence: LIELKVPDIGGHENVDVIAVEIKAGDTVNVDDTLVTLETDKATMDVPATAAGVVKEVKVAVGGKISEGGVIAVIE |
Sequence similarities
Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length598
- Mass (Da)62,656
- Last updated2022-10-12 v1
- Checksum6A012297CB114E0A
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP091521 EMBL· GenBank· DDBJ | UOP05094.1 EMBL· GenBank· DDBJ | Genomic DNA |