PTMD_PENSI
ID PTMD_PENSI Reviewed; 427 AA.
AC A0A140JWS8;
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=Indole diterpene prenyltransferase ptmD {ECO:0000303|PubMed:25831977};
DE EC=2.5.1.- {ECO:0000269|PubMed:25831977};
DE AltName: Full=Penitrem biosynthesis cluster 1 protein D {ECO:0000303|PubMed:25831977};
GN Name=ptmD {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: Indole diterpene prenyltransferase; part of the gene cluster
CC that 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 -!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family.
CC {ECO:0000305}.
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DR EMBL; LC027936; BAU61555.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A140JWS8; -.
DR SMR; A0A140JWS8; -.
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 ptmD"
FT /id="PRO_0000446559"
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; 48772 MW; 5513BB910463CEF4 CRC64;
MTNSLLTIGD MVQGVELPDA DRQFWWDSLA PILSRMLQCS KYSVESQANI LSFFKDFIVP
SYGPRPSIGG EFFWKSYVTY NHTPGQVSFN FHKDKCTVRL SNVPTAPLAG TASDPFNQKG
VVQTIKQIQK ALPDMDITLF DYFSEAFLVA DEDTVGLDAR KPVPQYNQLV VASMLGYDFE
PVPRVKVYFN PRWKALQMNT ENHDLIWTAI NNLGSPIKSY KRTLDLLQEC GTPRQLGGWI
FQPEFISFDL AENMSNAARL KLYGFTTKTC WSHIESIYTL DGRLNDAETQ RGLAVLKRLW
HLALSIPEDH DENQDLPPCP HLTAGVIYNY ELRENSAKPE AKIYIPVRFY GSGDGKVIEG
LVDFFKSEGW DELARSYQRD FVSVFSTPDG KMAGEHHDIS FSYKNEHPYV TAYYRPELIR
PMERHIV
