Protein: LTME_EPIFI
Sequence: MKPTTRCPFDYLVSQCGKHHFKTFVQLLSPLLQDEDPDRYALILDIMDAVHFSAILIDDIANQSALRRNQPAAHVVFGETETATRAYLVLLRVVNRTMRENPVLAGELLNSLEEIHQGQDESLVWRRDGLETFPVADDERLAAYVRMSRLKTGSLFVLLGRLLANGGTEFDDLLVRFGLYAQLQHDCKNIYSPEYALNKGSVAEDLRNGELSYPVVVALIENKAEGIVGEALRTRSDGDTEQALRVLESPAVKDACLHALEAASVGLEDLVEAWGRREKMRSDTLDGDDLTRPSTITQHEQDDHVDRAAIDAKSDASGSSNKSLTPPETAPTTDTLSETAVGDISSVDVDYWTRRCVPIIGSLLKSCRVYSEAERETQLRFLQEHVLPNLGPRPSSPGSQIQSMATFSGFPLQPSINLSGSGQAKVRYTFEPLDSLSGTEVDPFALAPAQRVLEKLSTLLGVWPGWIDALIAAYHPTREEVEQLHPNLHEYLRGVLVRTTGRQDVQVPPMPRMWVCFVALDLEGASQALKVYFDPKIKEAVTGIPSCKYTCQILRTVDRFGNAKAVDMLEQFLAEEHSIGAVELIAIDCVPEEMQPSARIKVYVHTMSNSFQTVRKYMTMGGRCMDPATLEGLENLHDVWYSLLGESQGIVNEEYSKPLTGFSSMQHHLYFSYEMTPGNADPGVKVYIPVQSYAPDDKTIAQNYEANFRQLNWPWGEPGVYEAVIESALGPVKHSRATFLHGGSSFIFSKGRGVYQSIYLDPPLEEGGNIAVFEHHDDQDTIVDLGNM
What is the function of this protein?
Multi-functional prenyltransferase; part of the gene cluster that mediates the biosynthesis of lolitrems, indole-diterpene mycotoxins that are potent tremorgens in mammals, and are synthesized by clavicipitaceous fungal endophytes in association with their grass hosts (PubMed:16765617, PubMed:22750140).  The geranylgeranyl diphosphate (GGPP) synthase ltmG is proposed to catalyze the first step in lolitrem biosynthesis (PubMed:16765617, PubMed:15991026).  LtmG catalyzes a series of iterative condensations of isopentenyl diphosphate (IPP) with dimethylallyl diphosphate (DMAPP), geranyl diphosphate (GPP), and farnesyl diphosphate (FPP), to form GGPP (PubMed:16765617, PubMed:15991026).  GGPP then condenses with indole-3-glycerol phosphate to form 3-geranylgeranylindole, an acyclic intermediate, to be incorporated into paxilline (PubMed:16765617).  Either ltmG or ltmC could be responsible for this step, as both are putative prenyl transferases (PubMed:16765617).  The FAD-dependent monooxygenase ltmM then catalyzes the epoxidation of the two terminal alkenes of the geranylgeranyl moiety, which is subsequently cyclized by ltmB, to paspaline (PubMed:16765617, PubMed:15991026).  The cytochrome P450 monooxygenases ltmQ and ltmP can sequentially oxidize paspaline to terpendole E and terpendole F (PubMed:22750140).  Alternatively, ltmP converts paspaline to an intermediate which is oxidized by ltmQ to terpendole F (PubMed:22750140).  LtmF, ltmK, ltmE and ltmJ appear to be unique to the epichloe endophytes (PubMed:16765617, PubMed:15991026).  The prenyltransferase ltmF is involved in the 27-hydroxyl-O-prenylation (PubMed:22750140).  The cytochrome P450 monooxygenase ltmK is required for the oxidative acetal ring formation (PubMed:22750140).  The multi-functional prenyltransferase ltmE is required for C20- and C21-prenylations of the indole ring of paspalanes and acts together with the cytochrome P450 monooxygenase ltmJ to yield lolitremanes by multiple oxidations and ring closures (PubMed:22750140).  The stereoisomer pairs of lolitriol and lolitrem N or lolitrem B and lolitrem F may be attributed to variations in the way in which ring closure can occur under the action of ltmJ (PubMed:22750140).  While the major product of this pathway is lolitrem B, the prenyl transferases and cytochrome P450 monooxygenases identified in this pathway have a remarkable versatility in their regio- and stereo-specificities to generate a diverse range of metabolites that are products of a metabolic grid rather than a linear pathway (PubMed:22750140).
What are the official names of this protein?
Multi-functional prenyltransferase ltmE, Lolitrem B biosynthesis cluster 3 protein E.
What is the protein family that this protein belongs to?
In the C-terminal section; belongs to the tryptophan dimethylallyltransferase family.