OME1B_MAGO7
ID OME1B_MAGO7 Reviewed; 498 AA.
AC G4MWB6;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=O-methyltransferase OME1 {ECO:0000303|PubMed:18433432};
DE EC=2.1.1.- {ECO:0000305|PubMed:18433432};
DE AltName: Full=ACE1 cytochalasan biosynthesis cluster protein OME1 {ECO:0000303|PubMed:29142718};
GN Name=OME1 {ECO:0000303|PubMed:18433432}; ORFNames=MGG_08377;
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: O-methyltransferase; part of the gene cluster that mediates
CC the biosynthesis of a tyrosine-derived cytochalasan acting as a fungal
CC signal recognized by resistant rice plants and leads to avirulence in
CC Pi33 resistant rice cultivars (PubMed:18433432). The first step in the
CC pathway is catalyzed by the hybrid PKS-NRPS ACE1, assisted by the enoyl
CC reductase RAP1, that are responsible for fusion of the tyrosine
CC precursor and the polyketide backbone (PubMed:29142718). The polyketide
CC synthase module (PKS) of ACE1 is responsible for the synthesis of the
CC polyketide backbone and the downstream nonribosomal peptide synthetase
CC (NRPS) amidates the carboxyl end of the polyketide with the tyrosine
CC precursor (PubMed:29142718). Because ACE1 lacks a designated
CC enoylreductase (ER) domain, the required activity is provided the enoyl
CC reductase RAP1 (PubMed:29142718). Reduction by the hydrolyase ORFZ,
CC followed by dehydration and intra-molecular Diels-Alder cyclization by
CC the Diels-Alderase ORF3 then yield the required isoindolone-fused
CC macrocycle (Probable). A number of oxidative steps catalyzed by the
CC tailoring enymes identified within the cluster, including cytochrome
CC P450 monooxygenases CYP1 to CYP4, the FAD-linked oxidoreductase OXR2
CC and the short-chain dehydrogenase/reductase OXR1, are further required
CC to 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 -!- PATHWAY: Secondary metabolite biosynthesis.
CC {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 class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01020}.
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DR EMBL; CM001232; EHA55876.1; -; Genomic_DNA.
DR RefSeq; XP_003715683.1; XM_003715635.1.
DR AlphaFoldDB; G4MWB6; -.
DR SMR; G4MWB6; -.
DR STRING; 318829.MGG_08377T0; -.
DR EnsemblFungi; MGG_08377T0; MGG_08377T0; MGG_08377.
DR GeneID; 2678552; -.
DR KEGG; mgr:MGG_08377; -.
DR VEuPathDB; FungiDB:MGG_08377; -.
DR eggNOG; KOG3178; Eukaryota.
DR HOGENOM; CLU_005533_1_2_1; -.
DR InParanoid; G4MWB6; -.
DR OMA; PVCIEFV; -.
DR OrthoDB; 817726at2759; -.
DR Proteomes; UP000009058; Chromosome 2.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR016461; COMT-like.
DR InterPro; IPR001077; O_MeTrfase_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00891; Methyltransf_2; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51683; SAM_OMT_II; 1.
PE 2: Evidence at transcript level;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..498
FT /note="O-methyltransferase OME1"
FT /id="PRO_0000449450"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 406
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 358
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 498 AA; 54893 MW; 50EC7E4FC7DFEF1D CRC64;
MSTMALHRTA STKSDTTMAC PNGLVKNLPL GGNTKCSACG SHRAEKRRAS STSSVSTTPT
SPSFSEADWS PLHNSSQEPQ PEYTKVANSL MRAITDYVGH LQNENLPMPS LEPAADAHGV
LKHPEGVAAR NAVVELAQRI VAMTMDPDMN LLISSLQFHF CSSLKVAIDL KVHEHVPRRG
SITSSELAAK VGADESILVR IMRALILKHV FCSPTPGTYA HTAMSWCMMK SPDAIDLLGH
RLDESFRASS RQADALALVN YREPDEADVK GFSMAFGTTE NFWEVLGHEG EEERAQRFNR
AMRAVSLNTL DVIPRMYPFD RIRGDGLLVD VGGGLGQVAR AIMGAHRGAG LRSCIVQDAH
AGDDAKKQPD VMEANRKLGV ELQKHNFFDP QPVKGASVYF LRHIFHDWPD RACVKILKQT
VEAMGKDSTL LICDQVVDDE ASPQATLYDI DMWSLFGGKE RNRSEWEALF RSADERLYIK
KVWTTAEAPT TMLEVCLS
