We previously constructed a heterologous production system for ergothioneine (ERG) in using five ERG biosynthesis genes () from . However, significant amounts of hercynine (HER), an intermediate of ERG, as ERG were accumulated, suggesting that the reaction of EgtB catalyzing the attachment of γ-glutamylcysteine (γGC) to HER to yield hercynyl-γ-glutamylcysteine sulfoxide was a bottleneck. In this study, we searched for other EgtBs and found many orthologs in diverse microorganisms. Among these, strains possessed EgtBs that catalyze the direct conversion of HER into hercynylcysteine sulfoxide with l-cysteine (l-Cys) as a sulfur donor, in a manner similar to those of acidobacterial CthEgtB and fungal Egt1. An study with recombinant EgtBs from and clearly showed that both enzymes accepted l-Cys but not γGC. We reconstituted the ERG production system in with from ; ERG productivity reached 657 mg L.
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