Halohydrin dehalogenases (HHDHs) (E.C.4.5.1.-) are bacterial lyases belonging to the superfamily of short-chain dehydrogenases/reductases (SDR). They catalyze the reversible dehalogenation of vicinal haloalcohols with epoxide formation. In the reverse reaction, i.e. epoxide ring opening, a variety of nucleophiles are accepted enabling the formation of new C-C, C-O, C-N and C-S bonds. Halohydrin dehalogenase HheG from Ilumatobacter coccineus was previously found to accept also sterically more demanding cyclic epoxides as well as acyclic non-terminal epoxide substrates. This special feature is based on HheG's broader active site compared to other structurally characterized HHDHs. We herein report the biochemical characterization of a new HheG homolog, HheG-682 from Actinobacteria bacterium, which has been identified via BLAST search in the nr protein sequence database of GenBank.