A0A397GUR8 · A0A397GUR8_9EURO
- ProteinNAD-dependent protein deacylase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids319 (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 | 29-48 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 73 | substrate | |||
Binding site | 76 | substrate | |||
Binding site | 107-110 | NAD+ (UniProtKB | ChEBI) | |||
Active site | 127 | Proton acceptor | |||
Binding site | 135 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 140 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 213 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 216 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 256-258 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 282-284 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 304 | 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 > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Fumigati
Accessions
- Primary accessionA0A397GUR8
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 4-319 | 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-73 and Arg-76) 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
- Length319
- Mass (Da)34,776
- Last updated2018-12-05 v1
- Checksum49DC44E60E2F748E
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
NKHV02000187 EMBL· GenBank· DDBJ | RHZ53408.1 EMBL· GenBank· DDBJ | Genomic DNA |