ID   CYP3B_MAGO7             Reviewed;         513 AA.
AC   G4MWB2;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Cytochrome P450 monooxygenase CYP3 {ECO:0000303|PubMed:18433432};
DE            EC=1.-.-.- {ECO:0000305|PubMed:18433432};
DE   AltName: Full=ACE1 cytochalasan biosynthesis cluster protein CYP3 {ECO:0000303|PubMed:29142718};
GN   Name=CYP3 {ECO:0000303|PubMed:18433432}; ORFNames=MGG_08379;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
RN   [2]
RP   FUNCTION, INDUCTION, AND PATHWAY.
RX   PubMed=18433432; DOI=10.1111/j.1469-8137.2008.02459.x;
RA   Collemare J., Pianfetti M., Houlle A.E., Morin D., Camborde L., Gagey M.J.,
RA   Barbisan C., Fudal I., Lebrun M.H., Boehnert H.U.;
RT   "Magnaporthe grisea avirulence gene ACE1 belongs to an infection-specific
RT   gene cluster involved in secondary metabolism.";
RL   New Phytol. 179:196-208(2008).
RN   [3]
RP   FUNCTION.
RX   PubMed=29142718; DOI=10.1039/c4sc03707c;
RA   Song Z., Bakeer W., Marshall J.W., Yakasai A.A., Khalid R.M., Collemare J.,
RA   Skellam E., Tharreau D., Lebrun M.H., Lazarus C.M., Bailey A.M.,
RA   Simpson T.J., Cox R.J.;
RT   "Heterologous expression of the avirulence gene ACE1 from the fungal rice
RT   pathogen Magnaporthe oryzae.";
RL   Chem. Sci. 6:4837-4845(2015).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=31644300; DOI=10.1021/acs.orglett.9b03372;
RA   Wang C., Becker K., Pfuetze S., Kuhnert E., Stadler M., Cox R.J.,
RA   Skellam E.;
RT   "Investigating the function of cryptic cytochalasan cytochrome P450
RT   monooxygenases using combinatorial biosynthesis.";
RL   Org. Lett. 21:8756-8760(2019).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of a tyrosine-derived cytochalasan acting as
CC       a fungal signal recognized by resistant rice plants and leads to
CC       avirulence in Pi33 resistant rice cultivars (PubMed:18433432,
CC       PubMed:31644300). The first step in the pathway is catalyzed by the
CC       hybrid PKS-NRPS ACE1, assisted by the enoyl reductase RAP1, that are
CC       responsible for fusion of the tyrosine precursor and the polyketide
CC       backbone (PubMed:29142718). The polyketide synthase module (PKS) of
CC       ACE1 is responsible for the synthesis of the polyketide backbone and
CC       the downstream nonribosomal peptide synthetase (NRPS) amidates the
CC       carboxyl end of the polyketide with the tyrosine precursor
CC       (PubMed:29142718). Because ACE1 lacks a designated enoylreductase (ER)
CC       domain, the required activity is provided the enoyl reductase RAP1
CC       (PubMed:29142718). Reduction by the hydrolyase ORFZ, followed by
CC       dehydration and intra-molecular Diels-Alder cyclization by the Diels-
CC       Alderase ORF3 then yield the required isoindolone-fused macrocycle
CC       (Probable). A number of oxidative steps catalyzed by the tailoring
CC       enymes identified within the cluster, including cytochrome P450
CC       monooxygenases CYP1 to CYP4, the FAD-linked oxidoreductase OXR2 and the
CC       short-chain dehydrogenase/reductase OXR1, are further required to
CC       afford the final cytochalasans that confer avirulence and which have
CC       still to be identified (Probable). The monooxygenase CYP1 has been
CC       shown to be a site-selective C-18 hydroxylase whereas the function of
CC       CYP3 is the site-selective epoxidation of the C-6/C-7 olefin that is
CC       present in some intermediate compounds (PubMed:31644300). Finally, SYN2
CC       and RAP2 are not required for avirulence in Pi33 resistant rice
CC       cultivars (PubMed:18433432). {ECO:0000269|PubMed:18433432,
CC       ECO:0000269|PubMed:29142718, ECO:0000269|PubMed:31644300,
CC       ECO:0000305|PubMed:18433432, ECO:0000305|PubMed:29142718}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:31644300, ECO:0000305|PubMed:18433432}.
CC   -!- INDUCTION: Expressed exclusively during fungal penetration of host
CC       leaves, the time point at which plant defense reactions are triggered.
CC       {ECO:0000269|PubMed:18433432}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CM001232; EHA55872.1; -; Genomic_DNA.
DR   RefSeq; XP_003715679.1; XM_003715631.1.
DR   AlphaFoldDB; G4MWB2; -.
DR   SMR; G4MWB2; -.
DR   EnsemblFungi; MGG_08379T0; MGG_08379T0; MGG_08379.
DR   GeneID; 2678569; -.
DR   KEGG; mgr:MGG_08379; -.
DR   VEuPathDB; FungiDB:MGG_08379; -.
DR   eggNOG; KOG0158; Eukaryota.
DR   HOGENOM; CLU_022195_0_2_1; -.
DR   InParanoid; G4MWB2; -.
DR   OMA; WNESALY; -.
DR   OrthoDB; 614788at2759; -.
DR   Proteomes; UP000009058; Chromosome 2.
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; 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   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..513
FT                   /note="Cytochrome P450 monooxygenase CYP3"
FT                   /id="PRO_0000449438"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         451
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   513 AA;  58346 MW;  F49140167E8A3713 CRC64;
     MLPRSLGHST SELSPPFDGP NGVERYVSET RSLLRKGYEK YLRRGVPFQM RNPVEELGAQ
     VVLPPKYLDE VKRAPTDLFS FEAYSEKAFL LNYSRAPRQT EAAAHIVRVD LTRNLGKLIT
     FYSDFAIFEV CLPLVLIRDL GALVTDLWNE SALYLDKTYN SEWQTKQAYE VVCGFVARVT
     SVAMVGAPLC RNPVWNRIVV ETTMASFGAA QAIKDKYSAR WRWLAPWSES IQKDLRRIRK
     ESIELLKPLY EDRKAAVSRS DDVQGSSEMF RDTLYWLITS NQKDRSLSGI TESQLFLSLA
     AIHTTSATLN SFVYDWIAHP EYHGEILAEV KETLAQVQLN GGKWTLQHVA MLRKLDSFMK
     ESARINPIGF VSIQRYTLKP YTFKDGFQLP AGVSFVFHSD GVHHDADNYP DPEKFDAYRH
     LHLRETVDPN RFHFASVSDS ALGFGAGNHA CPGRFLSAII MKFFLIQFMT AYEMKYEHGG
     IERLPNHDNS NTTAPNRTVN LLVRRCDGTS NNA