LTMF_EPIFI
ID LTMF_EPIFI Reviewed; 439 AA.
AC Q15FB3;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Indole diterpene prenyltransferase ltmF {ECO:0000303|PubMed:16765617};
DE EC=2.5.1.- {ECO:0000305|PubMed:16765617};
DE AltName: Full=Lolitrem B biosynthesis cluster 2 protein F {ECO:0000303|PubMed:16765617};
GN Name=ltmF {ECO:0000303|PubMed:16765617};
OS Epichloe festucae var. lolii (Neotyphodium lolii) (Acremonium lolii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Epichloe.
OX NCBI_TaxID=73839;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Lp19;
RX PubMed=16765617; DOI=10.1016/j.fgb.2006.04.004;
RA Young C.A., Felitti S., Shields K., Spangenberg G., Johnson R.D.,
RA Bryan G.T., Saikia S., Scott B.;
RT "A complex gene cluster for indole-diterpene biosynthesis in the grass
RT endophyte Neotyphodium lolii.";
RL Fungal Genet. Biol. 43:679-693(2006).
RN [2]
RP FUNCTION.
RC STRAIN=Lp19;
RX PubMed=15991026; DOI=10.1007/s00438-005-1130-0;
RA Young C.A., Bryant M.K., Christensen M.J., Tapper B.A., Bryan G.T.,
RA Scott B.;
RT "Molecular cloning and genetic analysis of a symbiosis-expressed gene
RT cluster for lolitrem biosynthesis from a mutualistic endophyte of perennial
RT ryegrass.";
RL Mol. Genet. Genomics 274:13-29(2005).
RN [3]
RP INDUCTION.
RX PubMed=20519633; DOI=10.1104/pp.110.158451;
RA Eaton C.J., Cox M.P., Ambrose B., Becker M., Hesse U., Schardl C.L.,
RA Scott B.;
RT "Disruption of signaling in a fungal-grass symbiosis leads to
RT pathogenesis.";
RL Plant Physiol. 153:1780-1794(2010).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=22750140; DOI=10.1016/j.febslet.2012.06.035;
RA Saikia S., Takemoto D., Tapper B.A., Lane G.A., Fraser K., Scott B.;
RT "Functional analysis of an indole-diterpene gene cluster for lolitrem B
RT biosynthesis in the grass endosymbiont Epichloe festucae.";
RL FEBS Lett. 586:2563-2569(2012).
CC -!- FUNCTION: Indole diterpene prenyltransferase; part of the gene cluster
CC that mediates the biosynthesis of lolitrems, indole-diterpene
CC mycotoxins that are potent tremorgens in mammals, and are synthesized
CC by clavicipitaceous fungal endophytes in association with their grass
CC hosts (PubMed:16765617, PubMed:22750140). The geranylgeranyl
CC diphosphate (GGPP) synthase ltmG is proposed to catalyze the first step
CC in lolitrem biosynthesis (PubMed:16765617, PubMed:15991026). LtmG
CC catalyzes a series of iterative condensations of isopentenyl
CC diphosphate (IPP) with dimethylallyl diphosphate (DMAPP), geranyl
CC diphosphate (GPP), and farnesyl diphosphate (FPP), to form GGPP
CC (PubMed:16765617, PubMed:15991026). GGPP then condenses with indole-3-
CC glycerol phosphate to form 3-geranylgeranylindole, an acyclic
CC intermediate, to be incorporated into paxilline (PubMed:16765617).
CC Either ltmG or ltmC could be responsible for this step, as both are
CC putative prenyl transferases (PubMed:16765617). The FAD-dependent
CC monooxygenase ltmM then catalyzes the epoxidation of the two terminal
CC alkenes of the geranylgeranyl moiety, which is subsequently cyclized by
CC ltmB, to paspaline (PubMed:16765617, PubMed:15991026). The cytochrome
CC P450 monooxygenases ltmQ and ltmP can sequentially oxidize paspaline to
CC terpendole E and terpendole F (PubMed:22750140). Alternatively, ltmP
CC converts paspaline to an intermediate which is oxidized by ltmQ to
CC terpendole F (PubMed:22750140). LtmF, ltmK, ltmE and ltmJ appear to be
CC unique to the epichloe endophytes (PubMed:16765617, PubMed:15991026).
CC The prenyltransferase ltmF is involved in the 27-hydroxyl-O-prenylation
CC (PubMed:22750140). The cytochrome P450 monooxygenase ltmK is required
CC for the oxidative acetal ring formation (PubMed:22750140). The multi-
CC functional prenyltransferase ltmE is required for C20- and C21-
CC prenylations of the indole ring of paspalanes and acts together with
CC the cytochrome P450 monooxygenase ltmJ to yield lolitremanes by
CC multiple oxidations and ring closures (PubMed:22750140). The
CC stereoisomer pairs of lolitriol and lolitrem N or lolitrem B and
CC lolitrem F may be attributed to variations in the way in which ring
CC closure can occur under the action of ltmJ (PubMed:22750140). While the
CC major product of this pathway is lolitrem B, the prenyl transferases
CC and cytochrome P450 monooxygenases identified in this pathway have a
CC remarkable versatility in their regio- and stereo-specificities to
CC generate a diverse range of metabolites that are products of a
CC metabolic grid rather than a linear pathway (PubMed:22750140).
CC {ECO:0000269|PubMed:15991026, ECO:0000269|PubMed:16765617,
CC ECO:0000269|PubMed:22750140}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:22750140}.
CC -!- INDUCTION: Expression is down-regulated when the stress-activated
CC mitogen-activated protein kinase (sakA) is deleted (PubMed:20519633).
CC {ECO:0000269|PubMed:20519633}.
CC -!- DISRUPTION PHENOTYPE: Leads to the accumulation of paspaline and 13-
CC desoxypaxilline, but also lolitriol and a small amount of lolitrem J
CC (PubMed:22750140). {ECO:0000269|PubMed:22750140}.
CC -!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family.
CC {ECO:0000305}.
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DR EMBL; DQ443465; ABF20224.1; -; Genomic_DNA.
DR AlphaFoldDB; Q15FB3; -.
DR SMR; Q15FB3; -.
DR GO; GO:0004659; F:prenyltransferase activity; IEA:UniProt.
DR GO; GO:0009820; P:alkaloid metabolic process; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR CDD; cd13929; PT-DMATS_CymD; 1.
DR InterPro; IPR033964; Aro_prenylTrfase.
DR InterPro; IPR017795; Aro_prenylTrfase_DMATS.
DR PANTHER; PTHR40627; PTHR40627; 1.
DR Pfam; PF11991; Trp_DMAT; 1.
DR SFLD; SFLDS00036; Aromatic_Prenyltransferase; 1.
DR TIGRFAMs; TIGR03429; arom_pren_DMATS; 1.
PE 2: Evidence at transcript level;
KW Transferase.
FT CHAIN 1..439
FT /note="Indole diterpene prenyltransferase ltmF"
FT /id="PRO_0000444328"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 264
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 350
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
SQ SEQUENCE 439 AA; 48987 MW; 463D896DBFD30530 CRC64;
MIAKNIELNG LDPATRALDI LYWKNHCIKQ LESLLCATDS YCTADKAAQL RILSELVLPN
LGPRPSNATG PSYLTRSGSP IMLSLNTTSS KNCVRYCWEI LGATGASNDD PLAVQVAKDV
VASLSATFRL STKWSETLLS NFAVTPDQAR QVINMLPEWI QGFVPEGMEC DFPKRIPFAM
TSFDLNGSNV AMKLYVNPRV KEILTGTPSS DLVWEFLRNL TPEMKPRAVD LLERFITDNS
GPSAIELVGI DCVDDAHLSN ARVKLYVHTM SSSFNTVKNY VTLGGAIWDE QTQKGLGILQ
SIWHLLLQEP EGISDNGFDK PVNDSSMLCQ KLYFSFELRP GTDFPQVKTY VPTWNYLRTD
GETIQNYEAI FRACDHPWGE DRTYGKIFQD AFGPATESRK KPIHCDASFL FTEETGVYQT
LYFSPPIEGE TEVQSNLVA
