Indole prenyltransferase; part of the gene cluster that mediates the biosynthesis of terrequinone A, an antitumor agent (PubMed:17704773, PubMed:16426969, PubMed:17291795, PubMed:22083274). The first step in the biosynthetic pathway for terrequinone A is formation of indole pyruvic acid (IPA) from L-tryptophan by the aminotransferase tdiD (PubMed:17704773). The nonribosomal peptide synthase tdiA then immediately converts unstable IPA to didemethylasterriquinone D (DDAQ D), via condensation of 2 IPA molecules (PubMed:17704773). The symmetric connectivity of the 2 IPA molecules is thought to arise by head-to-tail dual Claisen condensations facilitated by the TE domain (PubMed:17704773). TdiB then catalyzes reverse prenylation by transferring dimethylallyl diphosphate to carbon atom 2' of DDAQ D, to yield asterriquinone C-1 (PubMed:18029206). Finally, tdiC and tdiE enzymes robustly convert asterriquinone C-1 to terrequinone A via a transformation involving regular prenylation at carbon atom 5, which requires elimination of the hydroxy group on C-5 (PubMed:17704773, PubMed:18029206). Secondary metabolite biosynthesis. Specifically expressed at both asexual stages (PubMed:26773375). Expression is positively regulated by the secondary metabolism regulator laeA (PubMed:16426969, PubMed:17291795). Expression is also positively regulated by mpkB (PubMed:18378656). Expression is also positively regulated by mtfA (PubMed:24066102). Impairs the production of terrequinone A (PubMed:18029206). Belongs to the tryptophan dimethylallyltransferase family.