A0A2Z5JSU1 · A0A2Z5JSU1_9ACTN
- ProteinNAD-dependent protein deacetylase
- GenecobB1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids301 (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 | 39-59 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GAGLSTESGIPDYRGEGGSLS | ||||||
Binding site | 117-120 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: QNVD | ||||||
Active site | 135 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 143 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 146 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 194 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 197 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 234-236 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GSS | ||||||
Binding site | 278 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: L |
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 > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces
Accessions
- Primary accessionA0A2Z5JSU1
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 15-292 | Deacetylase sirtuin-type | ||||
Sequence: LPPGTTDLEPVADALGTGGVLVLSGAGLSTESGIPDYRGEGGSLSRHTPMTYQDFVGGAQARRRYWARSHLGWRTFGRAVPNAGHRAVAAFERHGLLAGVITQNVDGLHQAAGSEDVVELHGALDRVVCLSCGARSPRRELARRLEEANPGFEPVAAGINPDGDADLTDDQVAGFRVVPCTVCGGILKPDVVFFGETVPPQRVEHCRELVRAASSLLVLGSSLTVMSGLRFVRQAAQAGKPVLIVNRDPTRGDRHALTRVALPLGTALTTVADRLGIA |
Sequence similarities
Belongs to the sirtuin family. Class II subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length301
- Mass (Da)31,894
- Last updated2018-10-10 v1
- ChecksumE351C9E9D7F137B3
Keywords
- Technical term