G8YG66 · G8YG66_PICSO
- ProteinNAD-dependent protein deacylase
- GenePiso0_002864
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids301 (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 | 69 | substrate | |||
Binding site | 72 | substrate | |||
Binding site | 104-107 | NAD+ (UniProtKB | ChEBI) | |||
Active site | 124 | Proton acceptor | |||
Binding site | 132 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 137 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 194 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 197 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 238-240 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 286 | 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
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Debaryomycetaceae > Millerozyma
Accessions
- Primary accessionG8YG66
Proteomes
Subcellular Location
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 1-300 | 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-69 and Arg-72) 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.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length301
- Mass (Da)33,457
- Last updated2012-02-22 v1
- Checksum7B1BCC32EAC29A29
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
FO082051 EMBL· GenBank· DDBJ | CCE82165.1 EMBL· GenBank· DDBJ | Genomic DNA |