Microbial oxidoreductases are one of the most prevalent enzyme families widely distributed among the sequenced microorganisms. The broad annotations of those enzymes are not predictive of their substrate range as enzymes with high sequence similarity can catalyze chemical reactions with distinct substrates. In the absence of general <i>in-silico</i> rules for deducing substrate specificity of oxidoreductases, extensive and tedious screening of oxidoreductases encoded on a single bacterial genome is often required. Here, we identified the sequence fingerprints governing the substrate specificities of a microbial oxidoreductases by performing detailed bioinformatic analysis and mutagenesis studies. In addition, we also further evaluated the robustness of the discovered sequence fingerprints on additional oxidoreductases through substrate specificity testing. Our results expand the understanding of substrate specificity of microbial oxidoreductases, and serves as the basis for accurate functional predictions of uncharacterized proteins; thereby, providing insights for future rational enzyme design.

Discovery of sequence fingerprints governing substrate specificity in a microbial oxidoreductase

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