Acetyltransferase; part of the gene cluster that mediates the biosynthesis of erinacines, cyathane-xylosides that show unique biological activities, including leishmanicidal activity, stimulating activity for nerve growth-factor synthesis, and agonistic activity toward the kappa opioid receptor (PubMed:31535864). The geranylgeranyl diphosphate (GGPP) synthase eriE catalyzes the first step in erinacines biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (PubMed:31535864). GGPP is then substrate of the diterpene cyclase eriG for the production of cyatha-3,12-diene (PubMed:28371074). EriG is unable to use geranyl diphosphate (GPP) or farnesyl diphosphate (FPP) as substrates (PubMed:28371074). The cytochrome P450 monooxygenase eriI then hydroxylates cyatha-3,12-diene at C-14 of the seven-membered ring to produce erinacol, which is further hydroxylated at C-15 by the cytochrome P450 monooxygenase eriC to yield cyathadiol (PubMed:31535864). The cytochrome P450 monooxygenase eriA then catalyzes C-11 hydroxylation in the presence of the short chain dehydrogenase/reductase (SDR) eriH, which leads to the production of cyathatriol (PubMed:31535864). The acetyltransferase eriL converts cyathatriol into 11-O-acetyl-cyathatriol (PubMed:31535864). The SDR eriH catalyzes further oxidation of 11-O-acetyl-cyathatriol into 1-O-acetylcyathin A3 (PubMed:31535864). Finally, the glycosyl transferase eriJ tranfers xylose from UDP-xylose onto C-14 of 11-O-acetyl-cyathatriol to form eracine Q (PubMed:31535864). EriJ is also able to convert 11-O-acetyl-cyathatriol to eracine Q2 by using UDP-D-glucose as cosubstrate, but at a lower rate (PubMed:31535864). In the absence of eriL and eriJ, the SDR eriH is able to convert cyathatriol to cyathin A3; this is likely a switching mechanism in the biosynthesis of cyathins (C-14 ketogroup)and erinacines (C-14 glycosylated group) (PubMed:31535864). The roles of the SDR eriB, the polyprenyl transferase eriF and the dehydrogenase eriK have still to be identified (Probable). Secondary metabolite biosynthesis. Belongs to the wax synthase family.