The iron(II)/2-oxoglutarate (Fe/2OG) dependent oxygenase superfamily encompasses a variety of enzymes linked in their ability to activate chemically inert C-H bonds. In this work, we investigate Fe/2OG enzyme SadA, which natively hydroxylates N-succinyl amino acid substrates. We show that single active site substitutions can introduce new catalytic activity, namely the stereospecific halogenation and azidation of substrate. These results demonstrate the synthetic utility of Fe/2OG enzymes as reprogrammable catalysts for the functionalization of sp3 C-H bonds.