NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form (By similarity). Reactivates acetylated acetyl-CoA synthetase (ACS) through an NAD-dependent deacetylation. Is able to ADP-ribosylate itself. Involved in non-homologous end joining (NHEJ) repair of blunt, 5' overhang and 3' overhang DNA double strand breaks (DSB). H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide H2O + N(6)-succinyl-L-lysyl-[protein] + NAD(+) = 2''-O-succinyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide Binds 1 zinc ion per subunit. Inhibited by 2-hydroxy-1-naphthaldehyde and nicotinamide. Optimum pH is 9.0. Optimum temperature is 25 degrees Celsius. Interacts with both Ku and LigD; may form a trimeric complex during NHEJ. 2 residues (Tyr-53 and Arg-56) present in a large hydrophobic pocket are probably involved in substrate specificity. They are important for desuccinylation activity, but dispensable for deacetylation activity. Auto-ADP-ribosylated. Belongs to the sirtuin family. Class III subfamily.