OPR1_ORYSJ
ID OPR1_ORYSJ Reviewed; 380 AA.
AC Q84QK0; Q69TH2; Q84QJ9; Q8H9F1;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=12-oxophytodienoate reductase 1 {ECO:0000303|PubMed:17938955};
DE EC=1.3.1.42 {ECO:0000269|PubMed:12569412};
DE AltName: Full=12-oxophytodienoate-10,11-reductase 1 {ECO:0000303|PubMed:17938955};
DE Short=OPDA-reductase 1 {ECO:0000303|PubMed:12569412};
DE Short=OsOPR1 {ECO:0000303|PubMed:12569412};
GN Name=OPR1 {ECO:0000303|PubMed:12569412, ECO:0000303|PubMed:17938955};
GN Synonyms=OPDA, OPDA2, OPDAR1, OPR11 {ECO:0000303|PubMed:17938955},
GN OPR2 {ECO:0000303|PubMed:17938955}, RRJ4 {ECO:0000303|PubMed:12569412};
GN OrderedLocusNames=Os06g0216300, LOC_Os06g11290;
GN ORFNames=OsJ_20595 {ECO:0000312|EMBL:EAZ36274.1},
GN OSJNBb0024N18.13 {ECO:0000312|EMBL:BAD35834.1},
GN P0537F07.35 {ECO:0000312|EMBL:BAD35327.1};
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 [MRNA], AND INDUCTION.
RC STRAIN=cv. Nipponbare; TISSUE=Leaf;
RX PubMed=14559225; DOI=10.1016/j.bbrc.2003.09.123;
RA Agrawal G.K., Jwa N.-S., Shibato J., Han O., Iwahashi H., Rakwal R.;
RT "Diverse environmental cues transiently regulate OsOPR1 of the
RT 'octadecanoid pathway' revealing its importance in rice defense/stress and
RT development.";
RL Biochem. Biophys. Res. Commun. 310:1073-1082(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP INDUCTION BY JASMONATE.
RC STRAIN=cv. BL-1;
RX PubMed=12569412; DOI=10.1007/s00425-002-0909-z;
RA Sobajima H., Takeda M., Sugimori M., Kobashi N., Kiribuchi K., Cho E.M.,
RA Akimoto C., Yamaguchi T., Minami E., Shibuya N., Schaller F., Weiler E.W.,
RA Yoshihara T., Nishida H., Nojiri H., Omori T., Nishiyama M., Yamane H.;
RT "Cloning and characterization of a jasmonic acid-responsive gene encoding
RT 12-oxophytodienoic acid reductase in suspension-cultured rice cells.";
RL Planta 216:692-698(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=cv. Nipponbare;
RX PubMed=15215597; DOI=10.1271/bbb.68.1315;
RA Yamaguchi T., Nakayama K., Hayashi T., Yazaki J., Kishimoto N., Kikuchi S.,
RA Koike S.;
RT "cDNA microarray analysis of rice anther genes under chilling stress at the
RT microsporogenesis stage revealed two genes with DNA transposon Castaway in
RT the 5'-flanking region.";
RL Biosci. Biotechnol. Biochem. 68:1315-1323(2004).
RN [4]
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 [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [8]
RP INDUCTION BY JASMONATE.
RX PubMed=18071256; DOI=10.1271/bbb.70532;
RA Sobajima H., Tani T., Chujo T., Okada K., Suzuki K., Mori S., Minami E.,
RA Nishiyama M., Nojiri H., Yamane H.;
RT "Identification of a jasmonic acid-responsive region in the promoter of the
RT rice 12-oxophytodienoic acid reductase 1 gene OsOPR1.";
RL Biosci. Biotechnol. Biochem. 71:3110-3115(2007).
RN [9]
RP INDUCTION.
RX PubMed=18786507; DOI=10.1016/j.bbrc.2008.08.157;
RA Yara A., Yaeno T., Hasegawa M., Seto H., Seo S., Kusumi K., Iba K.;
RT "Resistance to Magnaporthe grisea in transgenic rice with suppressed
RT expression of genes encoding allene oxide cyclase and phytodienoic acid
RT reductase.";
RL Biochem. Biophys. Res. Commun. 376:460-465(2008).
RN [10]
RP FUNCTION, NOMENCLATURE, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=cv. Nipponbare;
RX PubMed=17938955; DOI=10.1007/s00425-007-0635-7;
RA Tani T., Sobajima H., Okada K., Chujo T., Arimura S., Tsutsumi N.,
RA Nishimura M., Seto H., Nojiri H., Yamane H.;
RT "Identification of the OsOPR7 gene encoding 12-oxophytodienoate reductase
RT involved in the biosynthesis of jasmonic acid in rice.";
RL Planta 227:517-526(2008).
CC -!- FUNCTION: Probably involved in the biosynthesis or metabolism of
CC oxylipin signaling molecules. In vitro, reduces cis(-)-12-
CC oxophytodienoic acid (cis(-)-OPDA) and to cis(-)-OPC-8:0.
CC {ECO:0000269|PubMed:12569412, ECO:0000269|PubMed:17938955}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + OPC-8 = (10Z,15Z)-12-oxophytodienoate + H(+) +
CC NADPH; Xref=Rhea:RHEA:21888, ChEBI:CHEBI:15378, ChEBI:CHEBI:15720,
CC ChEBI:CHEBI:57411, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.42;
CC Evidence={ECO:0000269|PubMed:12569412, ECO:0000269|PubMed:17938955};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21889;
CC Evidence={ECO:0000269|PubMed:12569412, ECO:0000269|PubMed:17938955};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q8LAH7};
CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis.
CC {ECO:0000269|PubMed:12569412, ECO:0000269|PubMed:17938955}.
CC -!- INDUCTION: By wounding, jasmonate, salicylate, salt, drought and cold
CC stresses, sucrose, copper, cadmium, mercury, UV-C, fungal elicitor and
CC ozone. {ECO:0000269|PubMed:12569412, ECO:0000269|PubMed:14559225,
CC ECO:0000269|PubMed:15215597, ECO:0000269|PubMed:18071256,
CC ECO:0000269|PubMed:18786507}.
CC -!- SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD35327.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD35835.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAD89605.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ557138; CAD89604.1; -; mRNA.
DR EMBL; AJ557139; CAD89605.1; ALT_INIT; mRNA.
DR EMBL; AB040743; BAC20139.1; -; mRNA.
DR EMBL; AB122088; BAD26703.1; -; Genomic_DNA.
DR EMBL; AP003525; BAD35326.1; -; Genomic_DNA.
DR EMBL; AP003525; BAD35327.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP004741; BAD35834.1; -; Genomic_DNA.
DR EMBL; AP004741; BAD35835.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008212; BAF19059.1; -; Genomic_DNA.
DR EMBL; AP014962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM000143; EAZ36274.1; -; Genomic_DNA.
DR RefSeq; XP_015643915.1; XM_015788429.1.
DR AlphaFoldDB; Q84QK0; -.
DR SMR; Q84QK0; -.
DR STRING; 39947.Q84QK0; -.
DR PaxDb; Q84QK0; -.
DR PRIDE; Q84QK0; -.
DR GeneID; 112936094; -.
DR KEGG; osa:4340490; -.
DR InParanoid; Q84QK0; -.
DR OrthoDB; 978998at2759; -.
DR BRENDA; 1.3.1.42; 4460.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000007752; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR Genevisible; Q84QK0; OS.
DR GO; GO:0016629; F:12-oxophytodienoate reductase activity; IDA:UniProtKB.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; TAS:Gramene.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009695; P:jasmonic acid biosynthetic process; IEP:Gramene.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IDA:UniProtKB.
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 1: Evidence at protein 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..380
FT /note="12-oxophytodienoate reductase 1"
FT /id="PRO_0000410707"
FT ACT_SITE 187
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9FUP0"
FT BINDING 35..37
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q8LAH7"
FT BINDING 68
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q8LAH7"
FT BINDING 110
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q8LAH7"
FT BINDING 182..185
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9FUP0"
FT BINDING 234
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q8LAH7"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9FUP0"
FT BINDING 305
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q8LAH7"
FT BINDING 326..327
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q8LAH7"
SQ SEQUENCE 380 AA; 42465 MW; AA89B8590ED6147F CRC64;
MVHAPAKVAA AAAIPLLTPY KMGQLELSHR VVLAPLTRCR SYGNVPQPHA AVYYSQRATR
GGLLIAEATD ISPTAQGYPE TPGIYTQQQI EAWKPIVDAV HRKGALFFLQ IWHVGRVSTT
DFQPNGQAPI SSTDKQITPD DSGMVYSKPR RLRTDEIPQI IDDFRRAARN AIEAGFDGVE
IHGAHGYLLE QFMKDSANDR TDEYGGSLEN RCRFAVEVID AVVAEVGAHR VGIRLSPFVD
FMDCFDSDPV ALGSYMVQQL NKHPGFLYCH MVEPRMAIIE GRRKIAHGLL PFRKQFNGTF
IAAGGYDREE GNKVVADGYA DLVAYGRLFL ANPDLPRRFE LDAPLNRYDR STFYTQDPVV
GYTDYPFLEE IDEESRTTYA
