A0A373LN00 · A0A373LN00_9FIRM
- ProteinNAD-dependent protein deacetylase
- GenecobB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids241 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
NAD-dependent protein deacetylase which modulates the activities of several enzymes which are inactive in their acetylated form.
Catalytic activity
- H2O + N6-acetyl-L-lysyl-[protein] + NAD+ = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 24 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 28 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 35 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 35 | nicotinamide (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 36 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 103 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 105 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 105 | nicotinamide (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 106 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 106 | nicotinamide (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 121 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 121 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 129 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 132 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 150 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 152 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 190 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 191 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 213 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 231 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: I |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | NAD+ binding | |
Molecular Function | NAD-dependent protein lysine deacetylase activity | |
Molecular Function | transferase activity | |
Molecular Function | zinc ion binding |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNAD-dependent protein deacetylase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Eubacteriales > Eubacteriaceae > Eubacterium
Accessions
- Primary accessionA0A373LN00
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-241 | Deacetylase sirtuin-type | ||||
Sequence: MEENIKKLKEIIDGSDNIVFFGGAGVSTESGVPDFRSVDGLYNQEYAYPPETILSHSFYRRNPEEFYRFYRNKMLFPSAEPNMAHKALAKLEEMGKLKAVITQNIDGLHQAAGSKNVYELHGSVHRNHCQDCGKFYGFDQVYEMEGIPRCQCGGIIKPDVVLYEEGLDQKTIQLSVEAIAKADVLIIGGTSLAVYPAAGLVDYYRGNKLVLINKSKTQKDQRADLVINQPIGEVLGQVVEL |
Sequence similarities
Belongs to the sirtuin family. Class U subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length241
- Mass (Da)26,882
- Last updated2018-11-07 v1
- Checksum4803BE7A188BA0B3
Keywords
- Technical term