Protein: PENI_PENTH
Sequence: MASLIGGSAIQHLAQDIDTNKINHKAKANGPNLAPKSRALDMVSKLEPSRGPVHEHWWDLTSPQLASMLEEAGYPVGRQLEILLFYNHTIPEADSSRNWQSLLPVTVVPLEYSWKWDTACESPEVRLTIEAFGDLSGTRADPLNQAAAIELLHRTKGVLPDLNQTWINHFCSTLFDEDKDKYMEEAQSGTGMRLQSTMLVAFEFGRTSTSTKTYLTPRRLGQQGFARLPEYMPAIQALGPSRALDTLMDFLHTSPEGVELTPFGLSFDNVEPTSSRLKFYFASPNTSYNSLREVLTLGCRISKANFNIEEKIRTIHSLAKALMVAPDNLPDDEHISARAQPQSLSSASDPVTSDIVKERTSLLAGYQYYFDIAPGADLPDIRFYAPIRKELINDRGVAAAVTDWMKAQGRGKFCDNYVRMLEGMAGERGLSKCHGLHSFIGCLIRRDGELDVTSYLLPG
What is the function of this protein?
Prenyltransferase; part of the gene cluster that mediates the biosynthesis of penigequinolones, potent insecticidal alkaloids that contain a highly modified 10-carbon prenyl group (PubMed:25859931).  The first stage is catalyzed by the nonribosomal pepdide synthetase penN that condenses anthranilic acid and O-methyl-L-tyrosine to produce 4'-methoxycyclopeptin (By similarity).  4'-methoxycyclopeptin is then converted to 4'-methoxydehydrocyclopeptin by the ketoglutarate-dependent dioxygenase penM through dehydrogenation to form a double bond between C-alpha and C-beta of the O-methyltyrosine side chain (By similarity).  PenM also converts its first product methoxydehydrocyclopeptin to 4'-methoxycyclopenin (By similarity).  The following conversion of 4'methoxycyclopenin into 4'-methoxyviridicatin is catalyzed by the cyclopenase penL (By similarity).  4'-methoxyviridicatin is the precursor of quinolone natural products, and is further converted to quinolinone B (Probable).  The prenyltransferase penI then catalyzes the canonical Friedel-Crafts alkylation of quinolinone B with dimethylallyl cation to yield dimethylallyl quinolone, which is subjected to FAD-dependent dehydrogenation by the FAD-linked oxidoreductase penH to yield conjugated aryl diene (PubMed:25859931).  The delta(3') double bond then serves as the site of the second alkylation with DMAPP catalyzed by the prenyltransferase penG to yield a carbenium ion intermediate, which can be attacked by H(2)O to yield a styrenyl quinolone containing a C3'-hydroxyprenyl chain, or undergo cyclization to yield yaequinolones J1 and J2 (PubMed:25859931).  The conversion of the styrenyl quinolone into the tetrahydrofuran-containing yaequinolone C is performed by the FAD-dependent monooxygenase penE and involves epoxidation of the terminal C7'-C8' olefin, followed by epoxide ring opening initiated by the C3' hydroxyl group (PubMed:25859931).  The predicted cysteine hydrolase penJ acts as an epoxide hydrolase that enhances the rate of the 5-exo-tet cyclization step, increasing the yield of yaequinolone C (PubMed:25859931, PubMed:28114276).  PenF catalyzes the cationic rearrangement of the epoxide formed by penE (before ring opening to produce yaequinolone C) into yaequinolone D (PubMed:28114276).  Finally, the short-chain dehydrogenase/reductase (SDR)-like reductase penD, catalyzes both the dehydration of yaequinolone D and the reduction of the resulting oxonium to yield penigequinolone (PubMed:28114276).
What are the official names of this protein?
Prenyltransferase penI, Penigequinolones biosynthesis cluster protein I.
What is the protein family that this protein belongs to?
Belongs to the tryptophan dimethylallyltransferase family.