Protein: NOTC_ASPVE
Sequence: MAIEESPTYAEPGPYEALSRFSSLTREDHRKWWEHTGPVLEKVLKDSGYELQSQYTYLYFVQQHLVPYLGTFPTRGEDEHRWQSNLTPYKVPYELSWNISNKVVRISWDPVCDASGTEADAFNKKAIHDCTRQIAQLSNTIVLDRYRILHQELVISDQEEQELLRRDDLPKSGRGQHNLAVDFQNGGIALKVYFYPYMKFLATGSPVEQLFFAAIEKIGTADIQEPVKMLRCFLSPSFDDGKPSVDQKVFPSLLACDLCDPSKSRIKYYVIDKWVKWERIASLWTIGGRRLEDPSCAKGLALLKELWDLLAIPEGDRGDIWPNLVLGQPPTHLMTTMANYTLSPASRFPEPQVYLTTFGMNDMAIMDALTAFYERAGLTDMAKSYKKNVQSYYPNLDLSQTNWVHEAISFSYRNSKPYLSVYYSPF
What is the function of this protein?
Prenyltransferase; part of the gene cluster that mediates the biosynthesis of notoamide, a fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2. 2. 2]diazaoctane core (PubMed:23213353).  The first step of notoamide biosynthesis involves coupling of L-proline and L-tryptophan by the bimodular NRPS notE', to produce cyclo-L-tryptophan-L-proline called brevianamide F (Probable).  The reverse prenyltransferase notF' then acts as a deoxybrevianamide E synthase and converts brevianamide F to deoxybrevianamide E via reverse prenylation at C-2 of the indole ring leading to the bicyclo[2. 2. 2]diazaoctane core (PubMed:22660767) (Probable).  Deoxybrevianamide E is further hydroxylated at C-6 of the indole ring, likely catalyzed by the cytochrome P450 monooxygenase notG', to yield 6-hydroxy-deoxybrevianamide E (Probable).  6-hydroxy-deoxybrevianamide E is a specific substrate of the prenyltransferase notC' for normal prenylation at C-7 to produce 6-hydroxy-7-prenyl-deoxybrevianamide, also called notoamide S (Probable).  As the proposed pivotal branching point in notoamide biosynthesis, notoamide S can be diverted to notoamide E through an oxidative pyran ring closure putatively catalyzed by either notH' cytochrome P450 monooxygenase or the notD' FAD-linked oxidoreductase (Probable).  This step would be followed by an indole 2,3-epoxidation-initiated pinacol-like rearrangement catalyzed by the notB' FAD-dependent monooxygenase leading to the formation of notoamide C and notoamide D (Probable).  On the other hand notoamide S is converted to notoamide T by notH' (or notD'), a bifunctional oxidase that also functions as the intramolecular Diels-Alderase responsible for generation of (-)-notoamide T (Probable).  To generate antipodal (+)-notoaminide T, notH (or notD) in Aspergillus strain MF297-2 is expected to catalyze a Diels-Alder reaction leading to the opposite stereochemistry (Probable).  The remaining oxidoreductase notD' (or notH') likely catalyzes the oxidative pyran ring formation to yield (-)-stephacidin A (Probable).  The FAD-dependent monooxygenase notI' is highly similar to notB' and is predicted to catalyze a similar conversion from (-)-stephacidin A to (+)-notoamide B via the 2,3-epoxidation of (-)-stephacidin A followed by a pinacol-type rearrangement (Probable).  Finally, it remains unclear which enzyme could be responsible for the final hydroxylation steps leading to notoamide A and sclerotiamide (Probable).
What are the official names of this protein?
6-Hydroxy-7-prenyldeoxybrevianamide E synthase notC', Notoamide biosynthesis cluster protein C', Prenyltransferase notC.
What is the protein family that this protein belongs to?
Belongs to the tryptophan dimethylallyltransferase family.