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. 2020 Aug 14;12(11):1975–1987. doi: 10.1093/gbe/evaa175

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© The Author(s) 2020. Published by Oxford University Press on behalf of the Society for Molecular Biology and Evolution.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Fig. 3. — Architecture of the PKS proteins from Profftella_Dco (Dip_Dco, shown in bold), with the predicted biosynthetic pathway for diaphorin in Profftella_Dco. For comparison, PKS orthologs from Profftella_DC (Dip_DC) and the Paederus symbiont (Ped) are shown in gray, above Dip_Dcos. A, nonribosomal peptide synthetase (NRPS) adenylation domain; C, NRPS condensation domain; DH, dehydratase; GNAT, GCN5-related N-acetyltransferase superfamily (usually serving as acetyltransferase in PKSs); ECH, enoyl-CoA reductase-like domain; KR, ketoreductase; KS, ketosynthase; KS⁰, nonelongating KS; MT, C-methyltransferase; PS, putative pyrane synthase; OXY, oxygenase; TE, thioesterase; ?, region of unknown function. The domains in gray are predicted to be inactive due to missing active-site residues. The small circles denote carrier protein domains including ACPs and PCPs (NRPS peptidyl carrier proteins). Unusually amplified ACPs in DipP_Dco and DipT_Dco are highlighted in red (see also supplementary text S1, Supplementary Material online).