A0A267T5W0 · A0A267T5W0_9BACT
- ProteinDihydrolipoyl dehydrogenase
- GenelpdA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids464 (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+ = H+ + N6-[(R)-lipoyl]-L-lysyl-[protein] + NADH
Cofactor
Note: Binds 1 FAD per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 51 | FAD (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 114 | FAD (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 180-187 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GSGAIGVE | ||||||
Binding site | 203 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 270 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 310 | FAD (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 443 | 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 > Bacteroidota > Cytophagia > Cytophagales > Flectobacillaceae > Flectobacillus
Accessions
- Primary accessionA0A267T5W0
Proteomes
PTM/Processing
Features
Showing features for disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Disulfide bond | 42↔47 | Redox-active | ||||
Sequence: CLNWGC |
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 5-325 | FAD/NAD(P)-binding | ||||
Sequence: YDLIVIGSGPGGYVAAIRASQLGLKCAVVERESLGGICLNWGCIPTKALLKSAQVFEYIKHASDYGITVSEASADFGAVIKRSRGVADSMSKGVQFLMKKNKIDVIMGNGKVKPGKKVEVTAADGAVTVYDAKNIMIATGARARALPNIPIDGVKVIDYRKAMSLESQPKSLVVIGSGAIGVEFAYVYAAMGTKVTIVEFMPNIVPVEDEDVSKELAKQYKKLGIDIHTNSSVESVDTAGEGCKVSVKTPSGNITIDCDIVLSAAGVISNLENVGLEDVGIITDKGKILVNQWYETNIPGYYAIGDVTPGPALAHVASAEG | ||||||
Domain | 345-453 | Pyridine nucleotide-disulphide oxidoreductase dimerisation | ||||
Sequence: IPGCTYCSPEIASVGLTEKKAKEAGYEIKVGKFPFVASGKATAAGARDGFVKVIFDAKYGEFLGAHMIGYNVTEMIAEVVVARRLETTAHEIMTAVHPHPTISEAIKGA |
Sequence similarities
Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length464
- Mass (Da)48,923
- Last updated2017-12-20 v1
- Checksum7195AC79E8477949
Keywords
- Technical term