A0A8T5IC00 · A0A8T5IC00_UNCEA
- ProteinNAD-dependent protein deacylase
- GenecobB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids484 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form. Deacetylates the N-terminal lysine residue of Alba, the major archaeal chromatin protein and that, in turn, increases Alba's DNA binding affinity, thereby repressing transcription.
Catalytic activity
- N6-acetyl-L-lysyl-[protein] + NAD+ + H2O = 2''-O-acetyl-ADP-D-ribose + nicotinamide + L-lysyl-[protein]
- N6-succinyl-L-lysyl-[protein] + NAD+ + H2O = 2''-O-succinyl-ADP-D-ribose + nicotinamide + L-lysyl-[protein]
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 113 | Nucleophile | ||||
Sequence: C | ||||||
Active site | 205 | |||||
Sequence: H | ||||||
Active site | 207 | |||||
Sequence: E | ||||||
Binding site | 259-278 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GAGISAESGLKTFRDNDGLW | ||||||
Binding site | 303 | substrate | ||||
Sequence: Y | ||||||
Binding site | 306 | substrate | ||||
Sequence: R | ||||||
Binding site | 337-340 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: QNVD | ||||||
Active site | 355 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 423-425 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GTS | ||||||
Binding site | 449-451 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: NLE | ||||||
Binding site | 467 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: A |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | NAD+ binding | |
Molecular Function | NAD-dependent histone deacetylase activity | |
Molecular Function | protein-malonyllysine demalonylase activity | |
Molecular Function | protein-succinyllysine desuccinylase activity | |
Molecular Function | transferase activity | |
Biological Process | glutamine metabolic process | |
Biological Process | protein deacetylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNAD-dependent protein deacylase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageArchaea > Euryarchaeota
Accessions
- Primary accessionA0A8T5IC00
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 233-481 | Deacetylase sirtuin-type | ||||
Sequence: ELAGSNILQNFARLALNKTPRVVVLTGAGISAESGLKTFRDNDGLWENHRLEDVASPIAWRRDPELVWRFYQARRRQLLEAEPNSAHYALAELENKVDSFTLITQNVDDLHSRAGSKNMVQMHGQLRLLRCEACYEIFEKMQTEDLEDDFITCQCEKGILRPHIVWFGEEPLGMMRIKRETMAADIFIVIGTSGVVYPANSLLPIAKSNGAYCIGVNLEAPGNVELFDEFHQGKAGEVLPELVEKLLQE |
Domain
2 residues (Tyr-303 and Arg-306) present in a large hydrophobic pocket are probably involved in substrate specificity. They are important for desuccinylation activity, but dispensable for deacetylation activity.
Sequence similarities
Belongs to the sirtuin family. Class III subfamily.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length484
- Mass (Da)53,763
- Last updated2022-10-12 v1
- Checksum233B6934DD1B866A