PEND_PENCR
ID PEND_PENCR Reviewed; 427 AA.
AC A0A0E3D8N4;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 24-JUN-2015, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=Indole diterpene prenyltransferase penD {ECO:0000303|PubMed:26213965};
DE EC=2.5.1.- {ECO:0000305|PubMed:26213965};
DE AltName: Full=Penitrem biosynthesis cluster protein D {ECO:0000303|PubMed:26213965};
GN Name=penD {ECO:0000303|PubMed:26213965};
OS Penicillium crustosum (Blue mold fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=36656;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, FUNCTION, AND PATHWAY.
RC STRAIN=PN2402;
RX PubMed=26213965; DOI=10.3390/toxins7082701;
RA Nicholson M.J., Eaton C.J., Starkel C., Tapper B.A., Cox M.P., Scott B.;
RT "Molecular cloning and functional analysis of gene clusters for the
RT biosynthesis of indole-diterpenes in Penicillium crustosum and P.
RT janthinellum.";
RL Toxins 7:2701-2722(2015).
CC -!- FUNCTION: Indole diterpene prenyltransferase; part of the gene cluster
CC that mediates the biosynthesis of the indole diterpenes penitrems
CC (PubMed:26213965). The geranylgeranyl diphosphate (GGPP) synthase penG
CC catalyzes the first step in penitrem biosynthesis via conversion of
CC farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl
CC pyrophosphate (GGPP) (Probable). Condensation of indole-3-glycerol
CC phosphate with GGPP by the prenyl transferase penC then forms 3-
CC geranylgeranylindole (3-GGI) (Probable). Epoxidation by the FAD-
CC dependent monooxygenase penM leads to a epoxidized-GGI that is
CC substrate of the terpene cyclase penB for cyclization to yield
CC paspaline (Probable). Paspaline is subsequently converted to 13-
CC desoxypaxilline by the cytochrome P450 monooxygenase penP, the latter
CC being then converted to paxilline by the cytochrome P450 monooxygenase
CC penQ (PubMed:26213965). Paxilline is converted to beta-paxitriol via C-
CC 10 ketoreduction by the short-chain dehydrogenase PC-15 which can be
CC monoprenylated at the C-20 by the indole diterpene prenyltransferase
CC penD (Probable). A two-step elimination (acetylation and elimination)
CC process performed by the O-acetyltransferase PC-16 and the
CC P.simplicissimum ptmI-ortholog not yet identified in P.crustosum, leads
CC to the production of the prenylated form of penijanthine (Probable).
CC The FAD-linked oxidoreductase ptmO then converts the prenylated form of
CC penijanthine into PC-M5 which is in turn transformed into PC-M4 by the
CC aromatic dimethylallyltransferase PC-22 (Probable). A series of
CC oxidation steps involving 4 cytochrome P450 monooxygenases (PC-21, PC-
CC 05, PC-23, PC-20) and a FAD-dependent monooxygenase (PC-14) are
CC required for the transformation of PC-M4 to penitrems A and E.
CC Synthesis of these final products is proposed to proceed via penitrems
CC D and C (PC-21, PC-05, PC-14) and penitrems B and F (PC-21, PC-05, PC-
CC 14, PC-23) (Probable). {ECO:0000269|PubMed:26213965,
CC ECO:0000305|PubMed:26213965}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:26213965}.
CC -!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family.
CC {ECO:0000305}.
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DR EMBL; KC963408; AGZ20194.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E3D8N4; -.
DR SMR; A0A0E3D8N4; -.
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..427
FT /note="Indole diterpene prenyltransferase penD"
FT /id="PRO_0000446558"
FT BINDING 77..78
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 259
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 263
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 344
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 409
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 413
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
SQ SEQUENCE 427 AA; 48885 MW; A6CBA3ECEC454B1C CRC64;
MTNSLLNNGD MVQGVELPDA DQQFWWDSLA PILSRMLQCS KYSVQSQANI LSFFKDFIVP
SYGPRPSIDG EFFWKSYVTY NHTPGQVSFN FHKNKCTVRL SNVPTAPLAG TASDPFNQKG
VVQTIKHIQK ALPGMDMTIF DYFSEAFLVA DEDTVGLDAR KPVPQYNQLV VASMLGYDFE
PVPRVKVYFN PRWKALQMNI ENHDLIWTAI NNLGSPIKSY KRTLDLLQEC GNPRQPGGWI
FQPEFISFDM GENMSNTARL KLYGFTTKTC WSHIESIYTL DRRLDDAETQ RGLAVLKRLW
HLALSIPEDH DENQDLPPCP HLTAGVIYNY ELRENSAKPE AKIYIPVRFY GSGDGKVIEG
LVDFFKSEGW DELATSYQRD FVSVFSTPDG KMVGEHHDIS FSYKNDHPYV TAYYRPELIR
PMERHIV
