CYP4B_MAGO7
ID CYP4B_MAGO7 Reviewed; 534 AA.
AC G4MWB3;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Cytochrome P450 monooxygenase CYP4 {ECO:0000303|PubMed:18433432};
DE EC=1.-.-.- {ECO:0000305|PubMed:18433432};
DE AltName: Full=ACE1 cytochalasan biosynthesis cluster protein CYP4 {ECO:0000303|PubMed:29142718};
GN Name=CYP4 {ECO:0000303|PubMed:18433432}; ORFNames=MGG_08378;
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; EHA55873.1; -; Genomic_DNA.
DR RefSeq; XP_003715680.1; XM_003715632.1.
DR AlphaFoldDB; G4MWB3; -.
DR SMR; G4MWB3; -.
DR EnsemblFungi; MGG_08378T0; MGG_08378T0; MGG_08378.
DR GeneID; 2678570; -.
DR KEGG; mgr:MGG_08378; -.
DR VEuPathDB; FungiDB:MGG_08378; -.
DR eggNOG; KOG0158; Eukaryota.
DR HOGENOM; CLU_022195_0_2_1; -.
DR InParanoid; G4MWB3; -.
DR OMA; KINACAF; -.
DR OrthoDB; 574756at2759; -.
DR Proteomes; UP000009058; Chromosome 2.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IGC:PAMGO_MGG.
DR GO; GO:0005506; F:iron ion binding; IGC:PAMGO_MGG.
DR GO; GO:0004497; F:monooxygenase activity; IGC:PAMGO_MGG.
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; 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.
PE 2: Evidence at transcript level;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..534
FT /note="Cytochrome P450 monooxygenase CYP4"
FT /id="PRO_0000449439"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 477
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 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 534 AA; 61603 MW; 6275EA4393D1F12C CRC64;
MLSLLETKII EPFMVVRQTL APLRLSRWQI FKHMTRILIF SSNTRTIIFC VLMSLVGYIV
SRIIWGRQEK YPDHGLPIVK TNDYHFDNIV AEGKRLYPNQ AFMGINKRYK FVIYPSSSWE
ELKRIPEQTA SIMDFQHVCN SGEWSLVGGE THELVKTITA ELTRSLPARV PNRQQDAKMT
FDTIIGHCPE EKGFNLLMTS LEIIAKINAC TFVGRELGAN KSWVTAVVYS PLWVYFAVTL
CNATPDILRP LLRPLFFLPA LRNYWNMQKL LKPKLDREME TFRQTDDKRK LLVPKSDQDL
PFTHFLLSRY TEAAATIKQL VIDYIQVSYT STPTTASALF HALWELAQHP EAAEVMRREL
ATVMIDGNLP KTHLQELKRM DSFLRESFRL HPITRFTLQR YVKEPFQLSD GSRIPPGVMA
VVDAQEINRS PEIWENPDEF DMDRFYRLRE ISGNDNRYHF VTTSSNSPGW GDGTQACPGR
FFATSTLKIV MAHIVMNYDV SLRKVAPLKS QPLVNGSYSP DDSVEIFFKS RNVE
