ID   RED3_MAGO7              Reviewed;         250 AA.
AC   G4N292;
DT   13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Short-chain dehydrogenase RED3 {ECO:0000303|PubMed:27902426};
DE            EC=1.1.1.- {ECO:0000305|PubMed:27902426};
DE   AltName: Full=Pyriculol/pyriculariol biosynthesis cluster protein RED3 {ECO:0000303|PubMed:27902426};
GN   Name=RED3 {ECO:0000303|PubMed:27902426}; ORFNames=MGG_10910;
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   IDENTIFICATION, INDUCTION, FUNCTION, AND PATHWAY.
RX   PubMed=27902426; DOI=10.1099/mic.0.000396;
RA   Jacob S., Groetsch T., Foster A.J., Schueffler A., Rieger P.H.,
RA   Sandjo L.P., Liermann J.C., Opatz T., Thines E.;
RT   "Unravelling the biosynthesis of pyriculol in the rice blast fungus
RT   Magnaporthe oryzae.";
RL   Microbiology 163:541-553(2017).
CC   -!- FUNCTION: Short-chain dehydrogenase; part of the gene cluster that
CC       mediates the biosynthesis of pyriculol and pyriculariol, two
CC       heptaketides that induce lesion formation upon application on rice
CC       leaves but are dispensable for pathogenicity (PubMed:27902426). The
CC       highly reducing polyketide synthase synthesizes the heptaketide
CC       backbone of pyriculol and pyriculariol (PubMed:27902426). Pyriculol and
CC       pyriculariol contain several hydroxyl moieties and double bonds, so it
CC       can be assumed that several reduction steps occur during biosynthesis.
CC       These reactions could be executed by PKS19 itself or partly by the
CC       tailoring enzymes OXR1, OXR2, RED1, RED2 or RED3, identified within the
CC       cluster (Probable). The FAD-linked oxidoreductase OXR1 is the only
CC       tailoring enzyme for which the function has been determined yet, and is
CC       involved in the oxidation of dihydropyriculol and dihydropyriculariol
CC       into pyriculol and pyriculariol, respectively (PubMed:27902426).
CC       {ECO:0000269|PubMed:27902426, ECO:0000305|PubMed:27902426}.
CC   -!- PATHWAY: Polyketide biosynthesis. {ECO:0000305|PubMed:27902426}.
CC   -!- INDUCTION: Expression is increased in rice-extract medium (REM) and is
CC       correlated with the production of pyriculol.
CC       {ECO:0000269|PubMed:27902426}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; CM001233; EHA52504.1; -; Genomic_DNA.
DR   RefSeq; XP_003712311.1; XM_003712263.1.
DR   AlphaFoldDB; G4N292; -.
DR   SMR; G4N292; -.
DR   STRING; 318829.MGG_10910T0; -.
DR   EnsemblFungi; MGG_10910T0; MGG_10910T0; MGG_10910.
DR   GeneID; 2677060; -.
DR   KEGG; mgr:MGG_10910; -.
DR   VEuPathDB; FungiDB:MGG_10910; -.
DR   eggNOG; KOG1611; Eukaryota.
DR   HOGENOM; CLU_010194_9_1_1; -.
DR   InParanoid; G4N292; -.
DR   OMA; WILPAYG; -.
DR   OrthoDB; 1259665at2759; -.
DR   Proteomes; UP000009058; Chromosome 3.
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..250
FT                   /note="Short-chain dehydrogenase RED3"
FT                   /id="PRO_0000446270"
FT   ACT_SITE        164
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         8..18
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         37..38
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         143..147
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         176..178
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
SQ   SEQUENCE   250 AA;  26296 MW;  B1BC3D46751D5B99 CRC64;
     MSKSTTVLIT GANKGIGLGM AKAYLSRPNH IVICSVRSAK TDVTDLEAAS KASGSKLLLV
     YIESTSKTDP AKAVEDVQAA GVDHLDVLIA NAGGMPEGNK PLLELGPDEL CWSVQVNAAA
     PLLVLQAFKP LLQKADAPRF AVISSTSGSI EHMKNIHSFI FPGYGAAKAT LNWLTMGVHL
     SQEWLTTLVI HPGLVQSEPG NWVAKQIGMA EAPTTIEQAA EGVIKALTNA TRESVGGKFL
     STSDGTVLPW