This enzyme belongs to the family of hydrolases, one of the largest known enzyme families comprising approximately 1% of the genes in the human genome, exists as a homodimer, and acts specifically on halide bonds in carbon-halide compounds.

Haloacetate dehalogenase is unique because it catalyzes the cleavage of the remarkably stable carbon–fluorine bond of a fluorinated aliphatic compound.

DL-2-Haloacid dehalogenase is unique in that a water molecule directly attacks the substrate, displacing the halogen atom.

Fluoroacetate is lethal to sheep and cattle at doses of 0.25 to 0.5 mg/kg of body weight, and is a problem in the livestock industry.

A fluoroacetate dehalogenase gene from the soil bacterium Moraxella species strain B was transferred into the rumen bacterium Butyrivibrio fibrisolvens and expressed in vitro at sufficiently high levels to detoxify fluoroacetate in the surrounding medium.