Histone deacetylases and histone-like deacetylases, classII
This subfamily includes bacterial as well as eukaryotic Class II histone deacetylase (HDAC) and related proteins. Deacetylases of class II are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues of histones (EC 3.5.1.98) and possibly other proteins to yield deacetylated histones/other proteins. Included in this family is a bacterial HDAC-like amidohydrolase (Bordetella/Alcaligenes species FB18817, denoted as FB188 HDAH) shown to be most similar in sequence and function to class II HDAC6 domain 3 or b (HDAC6b). FB188 HDAH is able to remove the acetyl moiety from acetylated histones, and can be inhibited by common HDAC inhibitors such as SAHA (suberoylanilide hydroxamic acid) as well as class II-specific but not class I specific inhibitors.
Comment:Active center contains inhibitor and a catalytic Zn ion that coordinates side chain atoms of two aspartates and one histidine, and a water molecule.
Comment:Bordetella sp. histone deacetylase homolog (FB188 HDAH) is able to remove the acetyl moiety from acetylated histones
Structure:1ZZ0: Bordetella sp. histone deacetylase homolog (FB188 HDAH) binds acetate and a Zn ion; contacts at 4.0A
Jiyao W et al.(2023). "The conserved domain database in 2023.",