F8QBF1 · F8QBF1_SERL3
- ProteinNAD-dependent protein deacylase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids285 (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 | 74 | substrate | |||
Binding site | 77 | substrate | |||
Binding site | 116-119 | NAD+ (UniProtKB | ChEBI) | |||
Active site | 141 | Proton acceptor | |||
Binding site | 149 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 152 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 188 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 191 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 226-228 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 252-254 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 270 | 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 > Basidiomycota > Agaricomycotina > Agaricomycetes > Agaricomycetidae > Boletales > Coniophorineae > Serpulaceae > Serpula
Accessions
- Primary accessionF8QBF1
Proteomes
Subcellular Location
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 1-285 | 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-74 and Arg-77) 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
- Length285
- Mass (Da)31,018
- Last updated2011-09-21 v1
- ChecksumE69D278CFE534CA9
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
GL945488 EMBL· GenBank· DDBJ | EGN94537.1 EMBL· GenBank· DDBJ | Genomic DNA |