ID   OXR1B_MAGO7             Reviewed;         349 AA.
AC   G4MVZ5;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Short-chain dehydrogenase/reductase OXR1 {ECO:0000303|PubMed:18433432};
DE            EC=1.1.1.- {ECO:0000305|PubMed:18433432};
DE   AltName: Full=ACE1 cytochalasan biosynthesis cluster protein OXR1 {ECO:0000303|PubMed:29142718};
GN   Name=OXR1 {ECO:0000303|PubMed:18433432}; ORFNames=MGG_08389;
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: Short-chain dehydrogenase/reductase; part of the gene cluster
CC       that mediates the biosynthesis of a tyrosine-derived cytochalasan
CC       acting as a fungal signal recognized by resistant rice plants and leads
CC       to 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   -!- 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 short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; CM001232; EHA55863.1; -; Genomic_DNA.
DR   RefSeq; XP_003715670.1; XM_003715622.1.
DR   AlphaFoldDB; G4MVZ5; -.
DR   SMR; G4MVZ5; -.
DR   STRING; 318829.MGG_08389T0; -.
DR   EnsemblFungi; MGG_08389T0; MGG_08389T0; MGG_08389.
DR   GeneID; 2678490; -.
DR   KEGG; mgr:MGG_08389; -.
DR   VEuPathDB; FungiDB:MGG_08389; -.
DR   eggNOG; KOG1208; Eukaryota.
DR   HOGENOM; CLU_010194_44_4_1; -.
DR   InParanoid; G4MVZ5; -.
DR   OMA; LNAGLWN; -.
DR   OrthoDB; 1076292at2759; -.
DR   Proteomes; UP000009058; Chromosome 2.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   2: Evidence at transcript level;
KW   NAD; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..349
FT                   /note="Short-chain dehydrogenase/reductase OXR1"
FT                   /id="PRO_0000449452"
FT   ACT_SITE        220
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         47..55
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         74..75
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         104..106
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         250..252
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
SQ   SEQUENCE   349 AA;  37898 MW;  CE1B22CBF14E1C7E CRC64;
     MSVPSFITAP EFEGGPPQGL SIPFRLRWSK THPPKEPIVT FKGRTVLVTG ANTGLGFEAA
     VKYAAFGADK IILAVRSIEK GEEAKKRIVE RTGRDATDIS VLKLDLGEYS SVKDFVSALH
     EVTPTLDVAL LNAGLGNPTY EKSSAGWEMA VQVNVLSTAL LAMLLLPLLR SSAAASGAKS
     HLTFVNSFAH TLVPRDFPLI EGSILKTATD ESSWNASSSY NIVKLLAMAS VQGFARMEAG
     EDQQRVIVNS VCPDLCETDL GRKFTGFISS IGKAIFYYLF ALSAEEGARC LIGATALGPE
     SHGRFWHHDF LYPFGELAQD QALMKKTWNE IIEAVGRDEP EILQLCRTT