A0A0L0NQP0 · A0A0L0NQP0_CANAR
- ProteinNAD-dependent protein deacylase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids293 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins. Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo.
Catalytic activity
- N6-glutaryl-L-lysyl-[protein] + NAD+ + H2O = 2''-O-glutaryl-ADP-D-ribose + nicotinamide + L-lysyl-[protein]
- N6-malonyl-L-lysyl-[protein] + NAD+ + H2O = 2''-O-malonyl-ADP-D-ribose + nicotinamide + L-lysyl-[protein]
- N6-succinyl-L-lysyl-[protein] + NAD+ + H2O = 2''-O-succinyl-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 | 67 | substrate | |||
Binding site | 70 | substrate | |||
Binding site | 102-105 | NAD+ (UniProtKB | ChEBI) | |||
Active site | 122 | Proton acceptor | |||
Binding site | 130 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 135 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 187 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 190 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 229-231 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 277 | NAD+ (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrion | |
Cellular Component | nucleus | |
Molecular Function | NAD+ binding | |
Molecular Function | NAD-dependent histone deacetylase activity | |
Molecular Function | protein-glutaryllysine deglutarylase activity | |
Molecular Function | protein-malonyllysine demalonylase activity | |
Molecular Function | protein-succinyllysine desuccinylase 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 deacylase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Metschnikowiaceae > Metschnikowiaceae incertae sedis > Candida/Metschnikowiaceae
Accessions
- Primary accessionA0A0L0NQP0
Proteomes
Organism-specific databases
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 1-293 | Deacetylase sirtuin-type | |||
Domain
In contrast to class I sirtuins, class III sirtuins have only weak deacetylase activity. Difference in substrate specificity is probably due to a larger hydrophobic pocket with 2 residues (Tyr-67 and Arg-70) that bind to malonylated and succinylated substrates and define the specificity.
Sequence similarities
Belongs to the sirtuin family. Class I subfamily.
Belongs to the sirtuin family. Class III subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length293
- Mass (Da)32,406
- Last updated2015-11-11 v1
- MD5 ChecksumA7D5D1C4E1557C98CB28DEC9B37648E1
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LGST01000056 EMBL· GenBank· DDBJ | KND96383.1 EMBL· GenBank· DDBJ | Genomic DNA |