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Glycoside phosphorylases in subfamily GH13_18 of the carbohydrate-active enzyme database CAZy catalyse the reversible phosphorolysis of α-glycosidic bonds. They contribute to a more energy-efficient metabolism  in vivo , and can be applied for the synthesis of valuable glucosides, sugars or sugar phosphates  in vitro . Continuing our efforts to uncover new phosphorylase specificities, we identified an enzyme from the myxobacterium  Corallococcus coralloides  DSM 2259 that does not feature the signature sequence patterns of previously characterised phosphorylases. The enzyme was recombinantly expressed and subjected to substrate screening. Although it was confirmed that the  Corallococcus  phosphorylase does not have the same substrate specificity as other phoshorylases from subfamily GH13_18, its true natural substrate remains a mystery for now. Myxobacteria have been widely investigated as producers of numerous bioactive secondary metabolites for decades, but little research has been conducted on myxobacterial proteins. The present study exemplifies the untapped metabolic activities and functional diversity that these fascinating organisms may have left to show.

A GH13 glycoside phosphorylase with unknown substrate specificity from Corallococcus coralloides