Identification of the new prenyltransferase Ubi-297 from marine bacteria and elucidation of its substrate specificity

Beilstein J Org Chem. 2022 Jun 22:18:722-731. doi: 10.3762/bjoc.18.72. eCollection 2022.


Aromatic prenylated metabolites have important biological roles and activities in all living organisms. Compared to their importance in all domains of life, we know relatively little about their substrate scopes and metabolic functions. Here, we describe a new UbiA-like prenyltransferase (Ptase) Ubi-297 encoded in a conserved operon of several bacterial taxa, including marine Flavobacteria and the genus Sacchromonospora. In silico analysis of Ubi-297 homologs indicated that members of this Ptase group are composed of several transmembrane α-helices and carry a conserved and distinct aspartic-rich Mg2+-binding domain. We heterologously produced UbiA-like Ptases from the bacterial genera Maribacter, Zobellia, and Algoriphagus in Escherichia coli. Investigation of their substrate scope uncovered the preferential farnesylation of quinoline derivatives, such as 8-hydroxyquinoline-2-carboxylic acid (8-HQA) and quinaldic acid. The results of this study provide new insights into the abundance and diversity of Ptases in marine Flavobacteria and beyond.

Keywords: Flavobacteria; Saccharomonospora; UbiA-like prenyltransferase; prenylation.

Grants and funding

We are grateful for financial support from the Leibniz Association. CB greatly acknowledges funding from the European Union’s Horizon 2020 research and innovation program (ERC Grant number: 802736, MORPHEUS). We are deeply thankful for funding by the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) under Project-ID 239748522 – CRC 1127 (projects A01 and A06).