A0A2B4EIV3 · A0A2B4EIV3_9BACI
- ProteinNAD-dependent protein deacetylase
- GenecobB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids245 (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
- N6-acetyl-L-lysyl-[protein] + NAD+ + H2O = 2''-O-acetyl-ADP-D-ribose + nicotinamide + L-lysyl-[protein]
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 26 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 30 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 37 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 37 | nicotinamide (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 38 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 105 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 107 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 107 | nicotinamide (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 108 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 108 | nicotinamide (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 123 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 123 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 131 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 134 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 151 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 154 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 190 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 191 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 216 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 234 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: I |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | NAD+ binding | |
Molecular Function | NAD-dependent histone deacetylase activity | |
Molecular Function | transferase activity | |
Molecular Function | zinc ion binding | |
Biological Process | protein deacetylation |
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 > Bacilli > Bacillales > Bacillaceae > Bacillus
Accessions
- Primary accessionA0A2B4EIV3
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-245 | Deacetylase sirtuin-type | ||||
Sequence: MIFVQQFEEVRSILEKAKKITVLTGAGASTESGIPDFRSANGLYADANVEMYLSRGYYNRSPKEFWKHYKEIFQINTFHQYKPNRGHRFLAEFEEQGKDITILTQNIDGLHQLGGSKHVIDLHGTLQTAHCPKCKAGYDLQYMIDHEVPRCQKCNFILNPDVVLYGDTLPQYQNAITRLYETDVFIVMGTSLKVQPVASFPQIAKREIGATTILVNEESTGQEYNFDFVFQNKIGEFVEGLSSMK |
Sequence similarities
Belongs to the sirtuin family. Class U subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length245
- Mass (Da)27,949
- Last updated2017-12-20 v1
- Checksum8B03C368420D49CD