OPR8_ORYSJ
ID OPR8_ORYSJ Reviewed; 406 AA.
AC Q0E0C6; A0A0P0VKL6; Q6YU32;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Putative 12-oxophytodienoate reductase 8;
DE EC=1.3.1.-;
DE AltName: Full=OPDA-reductase 8;
DE Short=OsOPR8;
GN Name=OPR8; Synonyms=OPR7; OrderedLocusNames=Os02g0559400, LOC_Os02g35310;
GN ORFNames=P0435E12.12;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
CC -!- FUNCTION: Putative oxophytodienoate reductase that may be involved in
CC the biosynthesis or metabolism of oxylipin signaling molecules.
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC -!- SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD16527.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AP005883; BAD16527.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP008208; BAF09062.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS79243.1; -; Genomic_DNA.
DR EMBL; AK069898; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015627742.1; XM_015772256.1.
DR AlphaFoldDB; Q0E0C6; -.
DR SMR; Q0E0C6; -.
DR STRING; 4530.OS02T0559400-01; -.
DR PaxDb; Q0E0C6; -.
DR PRIDE; Q0E0C6; -.
DR EnsemblPlants; Os02t0559400-01; Os02t0559400-01; Os02g0559400.
DR GeneID; 4329684; -.
DR Gramene; Os02t0559400-01; Os02t0559400-01; Os02g0559400.
DR KEGG; osa:4329684; -.
DR eggNOG; KOG0134; Eukaryota.
DR InParanoid; Q0E0C6; -.
DR OMA; PYSNCLD; -.
DR OrthoDB; 978998at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR ExpressionAtlas; Q0E0C6; baseline and differential.
DR Genevisible; Q0E0C6; OS.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001155; OxRdtase_FMN_N.
DR InterPro; IPR045247; Oye-like.
DR PANTHER; PTHR22893; PTHR22893; 1.
DR Pfam; PF00724; Oxidored_FMN; 1.
PE 2: Evidence at transcript level;
KW Fatty acid biosynthesis; Fatty acid metabolism; Flavoprotein; FMN;
KW Lipid biosynthesis; Lipid metabolism; NADP; Oxidoreductase;
KW Oxylipin biosynthesis; Reference proteome.
FT CHAIN 1..406
FT /note="Putative 12-oxophytodienoate reductase 8"
FT /id="PRO_0000410714"
FT ACT_SITE 223
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 67..69
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 218..221
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 270
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 361..362
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT CONFLICT 338
FT /note="A -> T (in Ref. 4; AK069898)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 406 AA; 45515 MW; EC1635CD5452180E CRC64;
MIRKKASPHC LHDVSGSCPH LSILLHSSRR PESAPVPCLL PMEAKIPLLT PHTMGRFHLA
HRVVHAPLTR SRCYNNLPQE HVQLYYSQRA TNGGLLIAEA TGVSETAQGY PNTPGIWTKE
QVEAWRTVVD AVHQKGGVFF CQIWHVGRAS TNDYQPNGQT PIPCTDKKIT PTVLKDGTVE
EFSAPRRLRE DEIPQIVDDF RIAARNCIEA GFDGVEIHCA FGYLIEQFMK DGVNDRTDKY
GGSIANRCRF ALEVIQAAID EIGSDRVGVR LSPYSNCLDC WDSDPDALGL YMIQAMSKLG
VLYCSMVEPE VVKVDGKVQI PYKLWHFRKV FAGTFIVAGG YNREEGNRAV SQGYTDLVAY
GKWFLANPDL PRRFELNAPL NKYDRSTFYT SDPVIGYTDY PFLSPL
