RED1_MAGO7
ID RED1_MAGO7 Reviewed; 284 AA.
AC G4N286;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Short-chain dehydrogenase RED1 {ECO:0000303|PubMed:27902426};
DE EC=1.1.1.- {ECO:0000305|PubMed:27902426};
DE AltName: Full=Pyriculol/pyriculariol biosynthesis cluster protein RED1 {ECO:0000303|PubMed:27902426};
GN Name=RED1 {ECO:0000303|PubMed:27902426}; ORFNames=MGG_12983;
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; EHA52498.1; -; Genomic_DNA.
DR RefSeq; XP_003712305.1; XM_003712257.1.
DR AlphaFoldDB; G4N286; -.
DR SMR; G4N286; -.
DR STRING; 318829.MGG_12983T0; -.
DR EnsemblFungi; MGG_12983T0; MGG_12983T0; MGG_12983.
DR GeneID; 5048918; -.
DR KEGG; mgr:MGG_12983; -.
DR VEuPathDB; FungiDB:MGG_12983; -.
DR eggNOG; KOG1209; Eukaryota.
DR HOGENOM; CLU_010194_2_9_1; -.
DR InParanoid; G4N286; -.
DR OMA; GPMRMVH; -.
DR OrthoDB; 1313182at2759; -.
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; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 2: Evidence at transcript level;
KW NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..284
FT /note="Short-chain dehydrogenase RED1"
FT /id="PRO_0000446268"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 10..19
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 38..39
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 57..59
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 151..155
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 184..186
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
SQ SEQUENCE 284 AA; 31489 MW; A148F280EED1B49E CRC64;
MGPGKEKFAL ITGCGDGGIG HALANNFVQN GFIVIATLLP HESRTHLEHA KIHVIDLDVT
KEDQMIPFRS TLEEITGGTL DVLVNNAGIC YTMTAADTDV KQVEKMFAVN VFGPMRLVHH
LHRMLIAAPR GVIVNIGSIG GVCPYVFGAS YNATKAALHH WGNTLRVEMK PFGVHVVNII
SGEVATNILK SDVRDNRTLP EDSVYAPLAQ LFKDHVNRTP DAMSPDDYAR GVVAMVQRRS
LPAWFWHGNA TGFIWTLDSF FPRTIWDWLF TRWFKLENLV GTQG
