ID   DPFGJ_GIBZE             Reviewed;         481 AA.
AC   I1RL13;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Cytochrome P450 monooxygenase dpfgJ {ECO:0000303|PubMed:32286350};
DE            EC=1.-.-.- {ECO:0000269|PubMed:32286350};
DE   AltName: Full=Diterpenoid pyrone biosynthesis cluster protein J {ECO:0000303|PubMed:32286350};
GN   Name=dpfgJ {ECO:0000303|PubMed:32286350};
GN   ORFNames=FG04590, FGRAMPH1_01T15651;
OS   Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS   / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=229533;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=17823352; DOI=10.1126/science.1143708;
RA   Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA   Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA   Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA   Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA   Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA   Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA   Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA   Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT   "The Fusarium graminearum genome reveals a link between localized
RT   polymorphism and pathogen specialization.";
RL   Science 317:1400-1402(2007).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=20237561; DOI=10.1038/nature08850;
RA   Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA   Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA   Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA   Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA   Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA   Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA   Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA   Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA   Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA   Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA   Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA   Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT   "Comparative genomics reveals mobile pathogenicity chromosomes in
RT   Fusarium.";
RL   Nature 464:367-373(2010).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA   King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA   Hammond-Kosack K.E.;
RT   "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT   graminearum.";
RL   BMC Genomics 16:544-544(2015).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND BIOTECHNOLOGY.
RX   PubMed=32286350; DOI=10.1038/s41467-020-15664-4;
RA   Tsukada K., Shinki S., Kaneko A., Murakami K., Irie K., Murai M.,
RA   Miyoshi H., Dan S., Kawaji K., Hayashi H., Kodama E.N., Hori A., Salim E.,
RA   Kuraishi T., Hirata N., Kanda Y., Asai T.;
RT   "Synthetic biology based construction of biological activity-related
RT   library of fungal decalin-containing diterpenoid pyrones.";
RL   Nat. Commun. 11:1830-1830(2020).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of diterpenoid pyrones (PubMed:32286350). The
CC       first step of the pathway is the synthesis of the alpha-pyrone moiety
CC       by the polyketide synthase dpfgA via condensation of one acetyl-CoA
CC       starter unit with 3 malonyl-CoA units and 2 methylations (Probable).
CC       The alpha-pyrone is then combined with geranylgeranyl pyrophosphate
CC       (GGPP) formed by the GGPP synthase dpfgD through the action of the
CC       prenyltransferase dpfgC to yield a linear alpha-pyrone diterpenoid
CC       (Probable). Subsequent steps in the diterpenoid pyrone biosynthetic
CC       pathway involve the decalin core formation, which is initiated by the
CC       epoxidation of the C10-C11 olefin by the FAD-dependent oxidoreductase
CC       dpfgE, and is followed by a cyclization cascade catalyzed by the
CC       terpene cyclase dpfgB (Probable). The short chain
CC       dehydrogenase/reductase dpfgG then oxidizes the 8S hydroxy group to a
CC       ketone and the short chain dehydrogenase/reductase dpfgH reduces the
CC       ketone to the 8R hydroxy group to yield higginsianin B
CC       (PubMed:32286350). Higginsianin B is further methylated by the
CC       methyltransferase dpfgI to produce the intermediate named FDDP B
CC       (PubMed:32286350). The cytochrome P450 monooxygenase dfgpJ then
CC       catalyzes a three-step oxidation at C-27 to generate a carboxylic acid
CC       as well as C-26 hydroxylation (PubMed:32286350). Finally,
CC       methyltransferase dpfgK methylates the carboxylic acid generated by
CC       dpfgJ, yielding the final diterpenoid pyrones from the pathway which
CC       were named FDDP D and FDDP E (PubMed:32286350).
CC       {ECO:0000269|PubMed:32286350, ECO:0000305|PubMed:32286350}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:32286350}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- BIOTECHNOLOGY: Diterpenoid pyrones display various biological
CC       activities and FDDP E shows anti-HIV activity (PubMed:32286350). FDDP D
CC       and FDDP E show also inhibitory activity of 42-mer-amyloid beta
CC       aggregation that is involved in the pathogenesis of Alzheimer's disease
CC       (PubMed:32286350). {ECO:0000269|PubMed:32286350}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; HG970333; CEF79625.1; -; Genomic_DNA.
DR   RefSeq; XP_011320991.1; XM_011322689.1.
DR   AlphaFoldDB; I1RL13; -.
DR   SMR; I1RL13; -.
DR   GeneID; 23551829; -.
DR   KEGG; fgr:FGSG_04590; -.
DR   VEuPathDB; FungiDB:FGRAMPH1_01G15651; -.
DR   eggNOG; KOG0158; Eukaryota.
DR   HOGENOM; CLU_001570_14_11_1; -.
DR   InParanoid; I1RL13; -.
DR   UniPathway; UPA00213; -.
DR   Proteomes; UP000070720; Chromosome 2.
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   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..481
FT                   /note="Cytochrome P450 monooxygenase dpfgJ"
FT                   /id="PRO_0000451556"
FT   TRANSMEM        23..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         427
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"
FT   CARBOHYD        338
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   481 AA;  53867 MW;  948EFA0A9B189DD6 CRC64;
     MEDLLDQVVV ELHRARSCLS DPLVFTQAAV IGSILFVFLL GLYNYFLHPI AHIKGPFLAA
     VTPISLIRAL RDIHNPGPDN HHYTKRGTSE DLILRFVFGA NNILLVDEGE DHKRLRGALQ
     PAFTAKAMRD QQDITHYHVQ KTVERLLEAA MDPSQTISLT KELNKLVWGN VGNLAFGEPA
     TLEQLENHEK AKDLHAQIAP ILEFFQYLNG NPILGRAARG LVGISRKVFG LSGNILGKDQ
     LRRHIASQQG QKNFLTAILG AKESSGLSFD EIHSNMLLLL MGGYDSSAAS LSAIFYHLLR
     EPQQYKRLQS ELHHAYSSVN DITCNSLLSQ PMLNACINES LRLVPPFNGH GSHRVTTSGT
     MIDGVWVPAG TLISADFYSL HRDPSCWAFP DEYRPERWLK EHQGPGTPFE NDVKTAWRPF
     SLGPRVCVGR EMALQSIRLA VSKIVYTFDM TLANRDFVWD RDAGSHYMWH DFDIAVTLAK
     A