PTME_PENSI
ID PTME_PENSI Reviewed; 425 AA.
AC A0A140JWU0;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 11-MAY-2016, sequence version 1.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=Aromatic prenyl transferase ptmE {ECO:0000303|PubMed:25831977};
DE EC=2.5.1.- {ECO:0000269|PubMed:25831977};
DE AltName: Full=Penitrem biosynthesis cluster 2 protein E {ECO:0000303|PubMed:25831977};
GN Name=ptmE {ECO:0000303|PubMed:25831977};
OS Penicillium simplicissimum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=69488;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, FUNCTION, AND PATHWAY.
RC STRAIN=AK-40;
RX PubMed=25831977; DOI=10.1002/anie.201501072;
RA Liu C., Tagami K., Minami A., Matsumoto T., Frisvad J.C., Suzuki H.,
RA Ishikawa J., Gomi K., Oikawa H.;
RT "Reconstitution of biosynthetic machinery for the synthesis of the highly
RT elaborated indole diterpene penitrem.";
RL Angew. Chem. Int. Ed. 54:5748-5752(2015).
CC -!- FUNCTION: Aromatic prenyl transferase; part of the gene cluster that
CC mediates the biosynthesis of the indole diterpenes penitrems
CC (PubMed:25831977). The geranylgeranyl diphosphate (GGPP) synthase ptmG
CC catalyzes the first step in penitrem biosynthesis via conversion of
CC farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl
CC pyrophosphate (GGPP) (PubMed:25831977). Condensation of indole-3-
CC glycerol phosphate with GGPP by the prenyl transferase ptmC then forms
CC 3-geranylgeranylindole (3-GGI) (PubMed:25831977). Epoxidation by the
CC FAD-dependent monooxygenase ptmM leads to a epoxidized-GGI that is
CC substrate of the terpene cyclase ptmB for cyclization to yield
CC paspaline (PubMed:25831977). Paspaline is subsequently converted to 13-
CC desoxypaxilline by the cytochrome P450 monooxygenase ptmP, the latter
CC being then converted to paxilline by the cytochrome P450 monooxygenase
CC ptmQ (PubMed:25831977). Paxilline is converted to beta-paxitriol via C-
CC 10 ketoreduction by the short-chain dehydrogenase ptmH which can be
CC monoprenylated at the C-20 by the indole diterpene prenyltransferase
CC ptmD (PubMed:25831977). A two-step elimination (acetylation and
CC elimination) process performed by the O-acetyltransferase ptmV and ptmI
CC leads to the production of the prenylated form of penijanthine
CC (PubMed:25831977). The FAD-linked oxidoreductase ptmO then converts the
CC prenylated form of penijanthine into PC-M5 which is in turn transformed
CC into PC-M4 by the aromatic dimethylallyltransferase ptmE
CC (PubMed:25831977). Five sequential oxidative transformations performed
CC by the cytochrome P450 monooxygenases ptmK, ptmU, ptmL, ptmN and ptmJ
CC yield the various penitrem compounds. PtmK, ptmU and ptmM are involved
CC in the formation of the key bicyclic ring of penitrem C via the
CC formation of the intermediates secopenitrem D and penitrem D. PtmL
CC catalyzes the epoxidation of penitrem D and C to yield penitrem B and
CC F, respectively. PtmJ catalyzes the last benzylic hydroxylation to
CC convert penitrem B to prenitrem E and penitrem F to penitrem A
CC (PubMed:25831977). {ECO:0000269|PubMed:25831977}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:25831977}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q50EL0}.
CC -!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family.
CC {ECO:0000305}.
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DR EMBL; LC027937; BAU61567.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A140JWU0; -.
DR SMR; A0A140JWU0; -.
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 InterPro; IPR012148; DMATS-type_fun.
DR PANTHER; PTHR40627; PTHR40627; 1.
DR Pfam; PF11991; Trp_DMAT; 1.
DR PIRSF; PIRSF000509; Trp_DMAT; 1.
DR SFLD; SFLDS00036; Aromatic_Prenyltransferase; 1.
DR TIGRFAMs; TIGR03429; arom_pren_DMATS; 1.
PE 3: Inferred from homology;
KW Transferase.
FT CHAIN 1..425
FT /note="Aromatic prenyl transferase ptmE"
FT /id="PRO_0000446560"
FT BINDING 83..84
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 92
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 198
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 265
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 269
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 345
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 410
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 414
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
SQ SEQUENCE 425 AA; 48751 MW; 883A85BB492E2499 CRC64;
MGSLSSPTDL TPYQVLSKYK KFPSPDEEFW WDHAASTLAD LIKWTKATPA QEYEFLQFFY
EHVIPNFSGY RPYDVPGRAW NTGITPSGLP LEYSVNWRNI DANAMVRVGV EPISQFAGTA
RDPYSHYKIW DTLNQLSQVK ALKSFDLELW RHFSSALCTS REEEALLDQT RTLPESFSIA
KMQHSMGFDF CDDEVVVKIY LIPNMKARAS GTPLAELLTG SIHAIYRDTI DRETLATVIN
YLDSTSNFND ATWFSFDCIP RSQSRIKLYG SDFRTTWSRA EDLWTVGGRY TDAVTMKGLA
YLKELWDLLP IQDFETLPEQ AVQNPPMLWA YEIRPGDKIP SPRIYIPGHC LNDKKVADGL
SAFFKRVGWS DLGDQYTDRL FSMFPKQDLK DSTALHTWIA FSYTEKSGVY MNCYYLASAS
FPFKL
