OXR1_MAGO7
ID OXR1_MAGO7 Reviewed; 507 AA.
AC G4N285;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 25-MAY-2022, entry version 46.
DE RecName: Full=FAD-linked oxidoreductase OXR1 {ECO:0000303|PubMed:27902426};
DE EC=1.-.-.- {ECO:0000269|PubMed:27902426};
DE AltName: Full=Pyriculol/pyriculariol biosynthesis cluster protein OXR1 {ECO:0000303|PubMed:27902426};
DE Flags: Precursor;
GN Name=OXR1 {ECO:0000303|PubMed:27902426}; ORFNames=MGG_10961;
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, DISRUPTION PHENOTYPE, CATALYTIC
RP ACTIVITY, 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 -!- CATALYTIC ACTIVITY:
CC Reaction=A + dihydropyriculol = AH2 + pyriculol; Xref=Rhea:RHEA:63972,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:17499, ChEBI:CHEBI:80728,
CC ChEBI:CHEBI:142635; Evidence={ECO:0000269|PubMed:27902426};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63973;
CC Evidence={ECO:0000269|PubMed:27902426};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + dihydropyriculariol = AH2 + pyriculariol;
CC Xref=Rhea:RHEA:63976, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:142636, ChEBI:CHEBI:142637;
CC Evidence={ECO:0000269|PubMed:27902426};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63977;
CC Evidence={ECO:0000269|PubMed:27902426};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q5BEJ5};
CC -!- PATHWAY: Polyketide biosynthesis. {ECO:0000269|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 -!- DISRUPTION PHENOTYPE: Impairs the production of pyriculol and
CC pyriculariol, but accumulates their reduced forms dihydropyriculol and
CC dihydropyriculariol. {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; EHA52497.1; -; Genomic_DNA.
DR RefSeq; XP_003712304.1; XM_003712256.1.
DR AlphaFoldDB; G4N285; -.
DR SMR; G4N285; -.
DR STRING; 318829.MGG_10961T0; -.
DR EnsemblFungi; MGG_10961T0; MGG_10961T0; MGG_10961.
DR GeneID; 2677715; -.
DR KEGG; mgr:MGG_10961; -.
DR VEuPathDB; FungiDB:MGG_10961; -.
DR eggNOG; ENOG502SJ3M; Eukaryota.
DR HOGENOM; CLU_018354_0_0_1; -.
DR InParanoid; G4N285; -.
DR OMA; DTINNGM; -.
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; 3.30.465.10; -; 1.
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 1: Evidence at protein level;
KW FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Reference proteome;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..507
FT /note="FAD-linked oxidoreductase OXR1"
FT /evidence="ECO:0000255"
FT /id="PRO_5003466490"
FT DOMAIN 73..245
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 507 AA; 54993 MW; 6B5587E53277A258 CRC64;
MTIKFASLIL AGLGLGSGAL GSVTFRREES SWTNDSLTSV FAQQAKGLFL PRTVISFQGQ
EWFENVTERW DIYAPPTFKV SVSPSTEKDV ESAVKLAAKF KIPFLATGGR HGYGTTLGKL
KNGLSIDLSL LNQFSIDSKA ATITVGPGVR FRDIFTPLYE AGFQVPTGTC SCVGMIGATL
GGGIGRLNGL DGLMIDALES ARVVTADGRT LTVSEKENKD LFWGMRGAGQ NFGVVVSATY
KLKPLYAAGV WTNVDLIFSP DKNATYFDVV TSMEVPPQLT IASVVTYNAT LDEPQLIATL
TWTGPRDEAL AAMKPILDVG PRHSEVTEAT YATLPRVATF GTTDAVCAPG QIYDIYGVGL
RRLDSAAWRS TFSKMARFYA AEPAGRASSI LYETWPVQAT VAVPDDATAY PWRDASTYVL
IQMRWDRPGS PLERAADRLG AELRSDLSAT GGYQGAGPAV YVNYAHGDER LEDIYGARKL
PRLAKLKKQY DPGNVFRFHH ALPTKYP
