Catalyzes the stereospecific hydrolysis of the cyclic amide bond of D-hydantoin. Has no activity on dihydropyrimidines. Binds 2 Zn(2+) ions per subunit. Can also use Ni(2+), Co(2+) or Mn(2+). Completely inhibited by p-chloromercuribenzoate and partially inhibited by metal chelating agents. The optimal activity is at pH 8.8 for manganese-containing form and pH 8.5 for cobalt-containing form. The oligomer is thermostable and retains full initial activity at 40-60 degrees Celsius. Homotetramer. Carboxylation allows a single lysine to coordinate two zinc ions. Belongs to the metallo-dependent hydrolases superfamily. Hydantoinase/dihydropyrimidinase family.