Polyamine deacetylase (PDAC), which acts preferentially on N(8)-acetylspermidine, and also on acetylcadaverine and acetylputrescine. Exhibits attenuated catalytic activity toward N(1),N(8)-diacetylspermidine and very low activity, if any, toward N(1)-acetylspermidine. Histone deacetylase activity has been observed in vitro. Has also been shown to be involved in MSH2 deacetylation. The physiological relevance of protein/histone deacetylase activity is unclear and could be very weak. May play a role in the promotion of late stages of autophagy, possibly autophagosome-lysosome fusion and/or lysosomal exocytosis in neuroblastoma cells. May play a role in homologous recombination. May promote DNA mismatch repair. H2O + N(8)-acetylspermidine = acetate + spermidine H2O + N-acetylputrescine = acetate + putrescine H2O + N-acetylcadaverine = acetate + cadaverine H2O + N(6)-acetyl-L-lysyl-[protein] = acetate + L-lysyl-[protein] Interacts with HDAC3. Interacts with HDAC2 and NCOR2/SMRT. Interacts with HSPA8/HSC70. Interacts with MSH2. Excluded from nucleoli. Belongs to the histone deacetylase family. HD type 2 subfamily. Protein/histone deacetylase activity in vivo is uncertain. The 3D structure analysis of the zebrafish ortholog shows that a glutamate gatekeeper and a sterically constricted active site confer specificity for N(8)-acetylspermidine hydrolysis and disfavour acetyllysine hydrolysis. Supporting this observation, has been shown to exhibit only very low activity, if any, towards acetyl-lysine peptide substrates. However, histone deacetylase activity has been observed in vitro and HDAC10 has also been shown to be involved in MSH2 deacetylation.