ID   JAND_PENJA              Reviewed;         438 AA.
AC   A0A0E3D8M5;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   24-JUN-2015, sequence version 1.
DT   03-AUG-2022, entry version 14.
DE   RecName: Full=Indole diterpene prenyltransferase janD {ECO:0000303|PubMed:26213965};
DE            EC=2.5.1.- {ECO:0000269|PubMed:26213965};
DE   AltName: Full=Penitrem biosynthesis cluster protein D {ECO:0000303|PubMed:26213965};
GN   Name=janD {ECO:0000303|PubMed:26213965};
OS   Penicillium janthinellum (Penicillium vitale).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=5079;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, FUNCTION, DISRUPTION
RP   PHENOTYPE, AND PATHWAY.
RC   STRAIN=PN2408;
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 janthitremanes
CC       such as shearinine K or shearinine A (PubMed:26213965). The
CC       geranylgeranyl diphosphate (GGPP) synthase janG catalyzes the first
CC       step in janthitremane biosynthesis via conversion of farnesyl
CC       pyrophosphate and isopentyl pyrophosphate into geranylgeranyl
CC       pyrophosphate (GGPP) (PubMed:26213965). Condensation of indole-3-
CC       glycerol phosphate with GGPP by the prenyl transferase janC then forms
CC       3-geranylgeranylindole (3-GGI) (PubMed:26213965). Epoxidation by the
CC       FAD-dependent monooxygenase janM leads to a epoxidized-GGI that is
CC       substrate of the terpene cyclase janB for cyclization to yield
CC       paspaline (PubMed:26213965). Paspaline is subsequently converted to 13-
CC       desoxypaspaline by the cytochrome P450 monooxygenase janP, via beta-PC-
CC       M6 in a series of alpha-face oxidations (Probable). The cytochrome P450
CC       monooxygenase janQ is proposed to carry out sequential beta-face
CC       oxidation steps at C-7 and C-13 of 13-desoxypaspaline to form
CC       paspalicine and paspalinine respectively (Probable). The indole
CC       diterpene prenyltransferase janD may then convert paspalinine into
CC       shearinine K which is substrate of janO and/or additional enzymes for
CC       oxidation and cyclization to generate shearinine A (Probable).
CC       {ECO:0000269|PubMed:26213965, ECO:0000305|PubMed:26213965}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:26213965}.
CC   -!- DISRUPTION PHENOTYPE: Abolishes the production of the janthitremanes
CC       shearinine A, F or K but accumulates 13-desoxypaxilline.
CC       {ECO:0000269|PubMed:26213965}.
CC   -!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; KF280651; AGZ20478.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0E3D8M5; -.
DR   SMR; A0A0E3D8M5; -.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR   GO; GO:0009820; P:alkaloid metabolic process; IEA:InterPro.
DR   CDD; cd13929; PT-DMATS_CymD; 1.
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   TIGRFAMs; TIGR03429; arom_pren_DMATS; 1.
PE   3: Inferred from homology;
KW   Transferase.
FT   CHAIN           1..438
FT                   /note="Indole diterpene prenyltransferase janD"
FT                   /id="PRO_0000446557"
FT   BINDING         80..81
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         190
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         268
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         350
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         414
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         418
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
SQ   SEQUENCE   438 AA;  49582 MW;  EA009D9C525E98AA CRC64;
     MGSHEVELRP WQSLAAGLGF SSPDEEYWWT AFAQPLNQLM EWADYSIAEQ YRVLAFLHRY
     VIPTCGPKPY RNGEQYWKTF MGFDHTPIQV SINFYNSKAT VRTANIPICA LSGSALDPIN
     QKATADTLKA QKHLAPGNDL RWFEHFAKAF FLPNDEAHLI NAKVSDRVLA MQGVQGMLSY
     DFPPNRTQTK VAMSPIWKHI ETGRPIGDLM IQSIKDLGDE ATGYMQSLQV LEEFIESEAA
     KDAGVSPAFF AFDTNLSENY KSSRIKIYLA TPRTAFNRMV DIFTLGGRLN GPEMDRATQA
     LRLLWSSVIN VPEGLLDNDD IVPKNPHRCA CVIFNFEIWP GASVPTPKIY LPAAYYGKPD
     LEIAEGMDVF FKSQGWNQPF HSYTDNYAKA FLRDQKVTCR HHDISFSYKG EGAYVTAYYK
     PELDAFADAA TWVPEIYK