ID   PTMN_PENSI              Reviewed;         600 AA.
AC   A0A140JWS7;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   11-MAY-2016, sequence version 1.
DT   25-MAY-2022, entry version 14.
DE   RecName: Full=Monooxygenase ptmN {ECO:0000303|PubMed:25831977};
DE            EC=1.-.-.- {ECO:0000269|PubMed:25831977};
DE   AltName: Full=Penitrem biosynthesis cluster 1 protein N {ECO:0000303|PubMed:25831977};
GN   Name=ptmN {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: Monooxygenase; part of the gene cluster that mediates the
CC       biosynthesis of the indole diterpenes penitrems (PubMed:25831977). The
CC       geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first
CC       step in penitrem biosynthesis via conversion of farnesyl pyrophosphate
CC       and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP)
CC       (PubMed:25831977). Condensation of indole-3-glycerol phosphate with
CC       GGPP by the prenyl transferase ptmC then forms 3-geranylgeranylindole
CC       (3-GGI) (PubMed:25831977). Epoxidation by the FAD-dependent
CC       monooxygenase ptmM leads to a epoxidized-GGI that is substrate of the
CC       terpene cyclase ptmB for cyclization to yield paspaline
CC       (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=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:25831977}.
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
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DR   EMBL; LC027936; BAU61554.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A140JWS7; -.
DR   SMR; A0A140JWS7; -.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000960; Flavin_mOase.
DR   InterPro; IPR020946; Flavin_mOase-like.
DR   Pfam; PF00743; FMO-like; 2.
DR   PIRSF; PIRSF000332; FMO; 1.
DR   PRINTS; PR00370; FMOXYGENASE.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase.
FT   CHAIN           1..600
FT                   /note="Monooxygenase ptmN"
FT                   /id="PRO_0000446589"
SQ   SEQUENCE   600 AA;  66951 MW;  B6679946A8363353 CRC64;
     MKVAVIGGGP SGLVTLKYLL AAHHFQPVDP IEVQLFESED RVGGTFSYRT YDRAELVSSA
     QLTTFSDYRW HDKSVDYLSA AEYVEYLEGY CDRFGLWPHI RLSTQVEKVE RTGKGKHRIT
     VSHDGQTSTW DCDAVAVCSG LHVKPNIPSI PGLDRVPVVF HSSEYKHVRQ LGQNTNVMVL
     GTGETGMDIA YFSVTADSTK STTVCHRNGF VIGPKRLPEI KLFGRVTSKT PGKALPVDLS
     RPYLFVNSYV HRKVRGTLQT TLSRWTVKAG SWLVTGTTRG FDQWVGSLPK DKYDESHYFY
     CKSTKAMPYI SAPYRSHSWV HRLRSSIIQA VLPDTGSRKI DLAPWPEYID EDGVVHFEKN
     SHPDSKVLLQ ERRFRPDVLV LATGYTQSFP FLGSDYCTPD HADQRGIWRT GDESVGYIGF
     VRPSFGAIPP LAEMQVQVWV LNLINRLPGP LVADDSYRLF SNPSGRIEYG VDHDMFAHRL
     ALDIGAAPSF FQALAHGWQV TVFWAMGGTL NTKFRLVGPW AWSGAPRIIC DELLDTVTGR
     RSTIELLTQL IMTAIVCGIP SILLFLADLL VALSIRIYQA ISVVSSRPSK GDSAVTENRG