A0A2M8T1Z4 · A0A2M8T1Z4_9BACI
- ProteinDihydrolipoyl dehydrogenase
- GenelpdA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids474 (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 | 51 | FAD (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 114 | FAD (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 151-153 | FAD (UniProtKB | ChEBI) | ||||
Sequence: TGS | ||||||
Binding site | 188-195 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GGGVIGIE | ||||||
Binding site | 211 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 280 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 320 | FAD (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 453 | 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 > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus
Accessions
- Primary accessionA0A2M8T1Z4
Proteomes
PTM/Processing
Features
Showing features for disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Disulfide bond | 42↔47 | Redox-active | ||||
Sequence: CLHKGC |
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 5-335 | FAD/NAD(P)-binding | ||||
Sequence: YDIVILGGGTGGYVAAIRAAQLGLKTAVVEKEKLGGTCLHKGCIPSKALLRSAEVYRTAREADQFGVETEGVSLNFEKVQQRKQAVVDKLAAGVNHLMKKGKIDVYNGYGRILGPSIFSPMPGTISVERGNGEENDMLIPKQVIIATGSRPRMLPGLEADGKYVLTSDEALQLEELPKSIIIVGGGVIGIEWASMLHDFGVKVTVIEYADRILPTEDQDISKEMESLLKKKGIQFVTGTKVLPDTMAKTSDDISIQAEKDGETVTYSAEKMLVSIGRQANIEGIGIENTDIVTENGVISVNENCQTKESHIYAIGDVIGGLQLAHVASHEG | ||||||
Domain | 355-464 | Pyridine nucleotide-disulphide oxidoreductase dimerisation | ||||
Sequence: VPKCIYSSPEAASVGLTEEEAKENGHNVKIGKFPFMAIGKALVYGESDGFVKIVADRDTDDILGVHMIGPHVTDMISEAGLAKVLDATPWEVGQTIHPHPTLSEAIGEAA |
Sequence similarities
Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length474
- Mass (Da)50,623
- Last updated2018-04-25 v1
- Checksum6FE4399C7495A45D