Chorismate mutase (CM) and cyclohexadienyl dehydratase (CDT) catalyze two subsequent reactions in the intracellular biosynthesis of phenylalanine. Surprisingly, exported CMs and CDTs exist in bacterial pathogens. Here, we report the discovery of novel and extremely rare exported bifunctional fusion enzymes, consisting of fused CM and CDT domains. Such enzymes were found in only nine bacterial species belonging to non-pathogenic γ- or β-proteobacteria. In γ-proteobacterial fusion enzymes, the CM domain is N-terminal to the CDT domain, whereas in β-proteobacteria the order is inversed. The CM domains share 15-20% sequence identity with the AroQγclass CM holotype ofMycobacterium tuberculosis(*MtCM), and the CDT domains 40-60% identity with the exported monofunctional enzyme ofPseudomonas aeruginosa(PheC).In vitrokinetics revealed aKm