CYP2B_MAGO7
ID CYP2B_MAGO7 Reviewed; 453 AA.
AC G4MWA8;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Cytochrome P450 monooxygenase CYP2 {ECO:0000303|PubMed:18433432};
DE EC=1.-.-.- {ECO:0000305|PubMed:18433432};
DE AltName: Full=ACE1 cytochalasan biosynthesis cluster protein CYP2 {ECO:0000303|PubMed:29142718};
GN ORFNames=MGG_15928;
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.
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). The
CC first step in the pathway is catalyzed by the hybrid PKS-NRPS ACE1,
CC assisted by the enoyl reductase RAP1, that are responsible for fusion
CC of the tyrosine precursor and the polyketide backbone
CC (PubMed:29142718). The polyketide synthase module (PKS) of ACE1 is
CC responsible for the synthesis of the polyketide backbone and the
CC downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl
CC end of the polyketide with the tyrosine precursor (PubMed:29142718).
CC Because ACE1 lacks a designated enoylreductase (ER) domain, the
CC 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:0000305|PubMed:18433432}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
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}.
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DR EMBL; CM001232; EHA55868.1; -; Genomic_DNA.
DR RefSeq; XP_003715675.1; XM_003715627.1.
DR AlphaFoldDB; G4MWA8; -.
DR SMR; G4MWA8; -.
DR EnsemblFungi; MGG_15928T0; MGG_15928T0; MGG_15928.
DR GeneID; 12986740; -.
DR KEGG; mgr:MGG_15928; -.
DR VEuPathDB; FungiDB:MGG_15928; -.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_022195_0_0_1; -.
DR InParanoid; G4MWA8; -.
DR OMA; YEMKWPD; -.
DR OrthoDB; 614788at2759; -.
DR Proteomes; UP000009058; 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 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 2: Evidence at transcript level;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..453
FT /note="Cytochrome P450 monooxygenase CYP2"
FT /id="PRO_0000449437"
FT TRANSMEM 13..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 397
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 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 453 AA; 52002 MW; B32820D331E7FE38 CRC64;
MKLRVSQSPT PQMVITMLHG SSTYSLLASK KRNSNVVGQY IKNGIPFRMR NPADPSQPQV
ILPFKYLSEM KNAAESSWSF MHFSNQSFLL EYINAPLGSS IAHQVVRGEL NKNLDWTALQ
PYMLFANTIA RTTSLVLAGP ELSANPEWTT IMVTFTMTLM QTSQEVRAKY SPWLRWLVPW
IHPGAKNLYK IRKRCAQLLA PSYQNRRAGM VGDEKPFMDA IQWLMNKRTY KSKDLMKLSD
DQLFLSVASI HSTSASTLST LYDLLDRPEC MDGILHEIRT IRAESKSSDW TKHDLDRLVK
LDSFMKESQR YHPVGQVTVQ RSNPRAYEFS DGLKIPANTQ TCFLSYELNH DPDVYPDPET
FDADRFLRMR EKVDPQKYHF AYVSEDSINF GAGAHSCPGR HFAANEIKLM LCELLLGYEM
KWPDGQSRPP TMFHDFSSNP NPGFDICIRE RRL
