A0A8J1TU13 · A0A8J1TU13_OWEFU
- ProteinNAD-dependent protein deacylase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids491 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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
- H2O + N6-glutaryl-L-lysyl-[protein] + NAD+ = 2''-O-glutaryl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide
- H2O + N6-malonyl-L-lysyl-[protein] + NAD+ = 2''-O-malonyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide
- H2O + N6-succinyl-L-lysyl-[protein] + NAD+ = 2''-O-succinyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 36-55 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GAGVSAESGVPTFRGAGGLW | ||||||
Binding site | 80 | substrate | ||||
Sequence: Y | ||||||
Binding site | 83 | substrate | ||||
Sequence: R | ||||||
Binding site | 118-121 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: QNID | ||||||
Active site | 136 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 144 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 147 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 185 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 190 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 227-229 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GTS | ||||||
Binding site | 253-255 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: NME | ||||||
Binding site | 271 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: A |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrion | |
Cellular Component | nucleus | |
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 | |
Molecular Function | zinc ion binding |
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
- Taxonomic lineageEukaryota > Metazoa > Spiralia > Lophotrochozoa > Annelida > Polychaeta > Sedentaria > Canalipalpata > Sabellida > Oweniida > Oweniidae > Owenia
Accessions
- Primary accessionA0A8J1TU13
Proteomes
Subcellular Location
Structure
Family & Domains
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-80 and Arg-83) that bind to malonylated and succinylated substrates and define the specificity.
Sequence similarities
Belongs to the sirtuin family. Class III subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length491
- Mass (Da)54,044
- Last updated2022-05-25 v1
- Checksum0D245378FD6F6F58
Keywords
- Technical term