CYP1B_MAGO7
ID CYP1B_MAGO7 Reviewed; 543 AA.
AC G4MVZ7;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Cytochrome P450 monooxygenase CYP1 {ECO:0000303|PubMed:18433432};
DE EC=1.-.-.- {ECO:0000269|PubMed:31644300};
DE AltName: Full=ACE1 cytochalasan biosynthesis cluster protein CYP1 {ECO:0000303|PubMed:29142718};
GN Name=CYP1 {ECO:0000303|PubMed:18433432}; ORFNames=MGG_08387;
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 -!- 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; EHA55865.1; -; Genomic_DNA.
DR RefSeq; XP_003715672.1; XM_003715624.1.
DR AlphaFoldDB; G4MVZ7; -.
DR SMR; G4MVZ7; -.
DR STRING; 318829.MGG_08387T0; -.
DR EnsemblFungi; MGG_08387T0; MGG_08387T0; MGG_08387.
DR GeneID; 2678617; -.
DR KEGG; mgr:MGG_08387; -.
DR VEuPathDB; FungiDB:MGG_08387; -.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_022195_0_2_1; -.
DR InParanoid; G4MVZ7; -.
DR OMA; NRFKFAN; -.
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; 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; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR SUPFAM; SSF48264; SSF48264; 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..543
FT /note="Cytochrome P450 monooxygenase CYP1"
FT /id="PRO_0000449436"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 478
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 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 517
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 543 AA; 61789 MW; 32421E8AD25CAAA7 CRC64;
MMTPTELITH YRIVQHSFAP LRLSWWETNR VIAVQIWRDS SFFTRILIAF IGLCLLSIFS
RLTRPRSLRR LGIPGAVQPR FSTWSLDFKK VLEDSAKKYP NSPFCLNAFG TEYAVLPSKC
YDEVKRLPEH QASAFAFFRE AFHGAWTGAG VQTPELGRTI AVELTRGIPS LVHWRQMDCA
EAFKMCIGEP SEWREIQLFE AIQRIVISVN SSSFVGRELG TNQNWLRLIY NMPLQLGIPT
VILGWTPFLL QPLLKPFLFA PLRMTQRKIK SMLRPVLEND VQEYEASSDK KNLLSPKEQG
KVQLTGWLLS RYKGKLDFEV LLQDFITVLF ESTPSTASTL FHVVCELAAD PALQDMLRQE
LEEHTDNGSL PQTHLNELRK MDSVMRESAR ASPFSYLVLY RKLSIPTKLS MGPELPAGTN
ICVDAHHINT SPDLWDQPHT FDGLRHYRAR QQPQNENRYK FANLGSDAPS WGDGLQACPG
RMFADNTIKI ILTHLLLNYD VKLRPGESKP EKGAMPNGSI VPDVWAKVLF RSRASSAVNE
GKK
