OXR2B_MAGO7
ID OXR2B_MAGO7 Reviewed; 584 AA.
AC G4MWA7;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 25-MAY-2022, entry version 42.
DE RecName: Full=FAD-linked oxidoreductase OXR2 {ECO:0000303|PubMed:18433432};
DE EC=1.-.-.- {ECO:0000305|PubMed:18433432};
DE AltName: Full=ACE1 cytochalasan biosynthesis cluster protein OXR2 {ECO:0000303|PubMed:29142718};
DE Flags: Precursor;
GN Name=OXR2 {ECO:0000303|PubMed:18433432}; ORFNames=MGG_15927;
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: FAD-linked oxidoreductase; 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=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
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 oxygen-dependent FAD-linked oxidoreductase
CC 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; EHA55867.1; -; Genomic_DNA.
DR RefSeq; XP_003715674.1; XM_003715626.1.
DR AlphaFoldDB; G4MWA7; -.
DR SMR; G4MWA7; -.
DR STRING; 318829.MGG_15927T0; -.
DR EnsemblFungi; MGG_15927T0; MGG_15927T0; MGG_15927.
DR GeneID; 12986739; -.
DR KEGG; mgr:MGG_15927; -.
DR VEuPathDB; FungiDB:MGG_15927; -.
DR eggNOG; ENOG502QQWK; Eukaryota.
DR HOGENOM; CLU_018354_4_4_1; -.
DR InParanoid; G4MWA7; -.
DR OMA; WWGDNYE; -.
DR OrthoDB; 317492at2759; -.
DR Proteomes; UP000009058; Chromosome 2.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.465.10; -; 2.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 2: Evidence at transcript level;
KW FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Reference proteome;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..584
FT /note="FAD-linked oxidoreductase OXR2"
FT /evidence="ECO:0000255"
FT /id="PRO_5003466222"
FT DOMAIN 128..310
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 584 AA; 63071 MW; 4435F90E2B55303A CRC64;
MRSIISAFIL SLNFCTQPLV RGAPSAADWQ ELQKAVEGRL FTAEPLARPC FSTFQGKSVE
PNVEECSTTK QHYLNSTFKT AAYAGFVHSY NEACASNVTD QCLLSADTFS TNGKNTSGTA
PLTGPCNLGM LSEKYIAVSR AEDVQAAFRF AHRTGMPLSV KATGHDYAAR SSLKGSLALW
TRQLNDIAFN PSFTPVGGSS SPIAAMTVGG GANLGEVYKF ADRHNVTFIG GSSGTVAAAG
GYSLLGGHGT LTPTYGMGAD RMLEATIVTP DGELRIANAH MNSDLFWALR GAGSATFGVV
LNATFKVEPV MPLTLALMSF NSTGANTGPF LSLLMKHTNI WAEEGWGGPM SMSTLALVNP
AMSVDAAKQS MKEVADYVSA QGGTVVLESL PSFYAFYTKY VEAASSTGTG AATFATFRTL
PKRLHQSEEG RAAMTKTFRD IKAAGHDTFI FQTTPNKFPY EPGSNAVHPS WRDSYWLVGT
SISWSSNDAG LEERMRVAAA VQEVSKNLTD LAPEGSMYPN EADPWTRNWA KEFWGEENYA
RLVQVKRKYD PHGLIGCWKC VGFEDKLMET ESAFRCLGAF QKKR
