PTMJ_PENSI
ID PTMJ_PENSI Reviewed; 515 AA.
AC A0A140JWT8;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 11-MAY-2016, sequence version 1.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=Cytochrome P450 monooxygenase ptmJ {ECO:0000303|PubMed:25831977};
DE EC=1.-.-.- {ECO:0000269|PubMed:25831977};
DE AltName: Full=Penitrem biosynthesis cluster 2 protein J {ECO:0000303|PubMed:25831977};
GN Name=ptmJ {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: Cytochrome P450 monooxygenase; 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 -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:25831977}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; LC027937; BAU61565.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A140JWT8; -.
DR SMR; A0A140JWT8; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
PE 3: Inferred from homology;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..515
FT /note="Cytochrome P450 monooxygenase ptmJ"
FT /id="PRO_0000446577"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 449
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
SQ SEQUENCE 515 AA; 57838 MW; 0F59BC29DEE84EA2 CRC64;
MMRDSLGPFR TFTLLTVGLL LSLFVIKTVK HRRRYHGLPT PPHNMLLGNL GVVLAEILAS
PEGFFHLFCV ENIRRKYNMP SVFYLDLWPI LPSIMVVAEP VVAKHMTQVQ PLQRERFSPN
LFSPLLTAEF ILAMEQKNWK KENPALNAAL TSTRVNEATS LLFPSLHSLR SRLHSISQSG
KQYPIKDLLI SYIIEVGGVI QLGGSFDLLA ETSALDPIIK QSLDMMGWNP VKRYICSKEI
KQRTDCLNRV LVATVQNTVQ TGESGMMSQS PIYLAHVEQL ASGRMDHAES IAYLVNTMKV
IILASVVTAG AASYCYLFLH KYPDCLREMR EEHDRVFSPD RTQTWELLQK EPHRINSLHF
TLAVVKETLR LIGVGGVFKK LKTEEFLETE GNVYPVVCNV AFICHLAMGR RADLFPDPDA
FRPHRFLPGA NPPIPADSFR PFEKGQLSCP GQTLALKSLV LLLLTTSREF DLVPVFPKGA
PRAAEYLGGE GYPEFHIGPH VNKGMPVMVH TRVDA
