OXR2_MAGO7
ID OXR2_MAGO7 Reviewed; 520 AA.
AC G4N287;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=FAD-linked oxidoreductase OXR2 {ECO:0000303|PubMed:27902426};
DE EC=1.-.-.- {ECO:0000305|PubMed:27902426};
DE AltName: Full=Pyriculol/pyriculariol biosynthesis cluster protein OXR2 {ECO:0000303|PubMed:27902426};
DE Flags: Precursor;
GN Name=OXR2 {ECO:0000303|PubMed:27902426}; ORFNames=MGG_16812;
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: FAD-linked oxidoreductase; 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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q5BEJ5};
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 oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; CM001233; EHA52499.1; -; Genomic_DNA.
DR RefSeq; XP_003712306.1; XM_003712258.1.
DR AlphaFoldDB; G4N287; -.
DR SMR; G4N287; -.
DR STRING; 318829.MGG_16812T0; -.
DR EnsemblFungi; MGG_16812T0; MGG_16812T0; MGG_16812.
DR GeneID; 12984968; -.
DR KEGG; mgr:MGG_16812; -.
DR VEuPathDB; FungiDB:MGG_16812; -.
DR eggNOG; ENOG502SJ3M; Eukaryota.
DR HOGENOM; CLU_018354_0_1_1; -.
DR InParanoid; G4N287; -.
DR OMA; TGSCGCV; -.
DR OrthoDB; 350817at2759; -.
DR Proteomes; UP000009058; Chromosome 3.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..520
FT /note="FAD-linked oxidoreductase OXR2"
FT /evidence="ECO:0000255"
FT /id="PRO_5003465654"
FT DOMAIN 79..251
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 520 AA; 56591 MW; EA22B82227CE8B10 CRC64;
MKSFSLLASA GLATLASLPL TMAGVITPSY FDKHPLSRRQ LSDAQVQREL GPQLSRGATI
IGPGGPGWDD AIERFDNESR PTIRLVVVPA VESDIATVVK LANRFGIPFL VKNRGHALTN
TIGRFRGIQI DMSRLTTITI QPGEPAESAW FQGGAWDKQA IEYLWDRGYV TVTGSCDCVG
MMGPGLGGGH GRYQGLYGLI SDNLINMNVV LADGSAVRVN ATSNPDLWWG MQGAGHNLGI
VTSFQSKIYP RKIDTWHYHS YTYTQDKLEA VFGALNTFHG NGDGSTPVLM GLNTGGFYID
PSVSQTEPVV SWVFGYAGPA SEAEALLEPF SRLGPAAEQS GDVPYPGVAT AMGTGQDQPL
CQPGDAHVQV TSQFNVYNAT AERALYQLFN RTIAAHPQLA DSVAFHEGYS TAAVDRADPS
ASAVAFRDRK LLMFFDARLK PADAADPEVL GMAREFGRQV RRIWNEGAPD LKPATYVNYA
AGDEPLESMY GYDAARLRRL RNIKRKYDPH GRFVYYNPIA
