OPR7_ORYSJ
ID OPR7_ORYSJ Reviewed; 394 AA.
AC Q6Z965; A0A0P0XGE5;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=12-oxophytodienoate reductase 7 {ECO:0000303|PubMed:17938955};
DE EC=1.3.1.42 {ECO:0000269|PubMed:17938955};
DE AltName: Full=12-oxophytodienoate-10,11-reductase 7 {ECO:0000305};
DE Short=OPDA-reductase 7 {ECO:0000303|PubMed:17938955};
DE Short=OsOPR7 {ECO:0000303|PubMed:17938955};
DE AltName: Full=Protein OPEN GLUME 1 {ECO:0000303|PubMed:29177846};
GN Name=OPR7 {ECO:0000303|PubMed:17938955};
GN Synonyms=OG1 {ECO:0000303|PubMed:29177846},
GN OPR13 {ECO:0000303|PubMed:18786507}, OPR3 {ECO:0000303|PubMed:18786507};
GN OrderedLocusNames=Os08g045960 {ECO:0000312|EMBL:BAT05755.1},
GN LOC_Os08g35740 {ECO:0000305};
GN ORFNames=OsJ_27573 {ECO:0000312|EMBL:EAZ42984.1},
GN P0493A04.35 {ECO:0000312|EMBL:BAD09599.1},
GN P0690E03.3 {ECO:0000312|EMBL:BAD09954.1};
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 [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 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 [5]
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).
RN [6]
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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND INDUCTION.
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).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29177846; DOI=10.1007/s00299-017-2232-y;
RA Li X., Wang Y., Duan E., Qi Q., Zhou K., Lin Q., Wang D., Wang Y., Long W.,
RA Zhao Z., Cheng Z., Lei C., Zhang X., Guo X., Wang J., Wu C., Jiang L.,
RA Wang C., Wan J.;
RT "OPEN GLUME1: a key enzyme reducing the precursor of JA, participates in
RT carbohydrate transport of lodicules during anthesis in rice.";
RL Plant Cell Rep. 37:329-346(2018).
CC -!- FUNCTION: Involved in the biosynthesis of jasmonate (JA) and perhaps in
CC biosynthesis or metabolism of other oxylipin signaling moleclules
CC (PubMed:17938955, PubMed:29177846). In vitro, reduces cis(+)-12-
CC oxophytodienoic acid (cis(+)-OPDA) and cis(-)-OPDA to cis(+)-OPC-8:0
CC and cis(-)-OPC-8:0, respectively (PubMed:17938955). May be required for
CC the spatial and temporal regulation of JA levels during dehiscence of
CC anthers, promoting the stomium degeneration program (PubMed:17938955).
CC Involved in carbohydrate transport underlying normal lodicule function
CC during anthesis (PubMed:29177846). {ECO:0000269|PubMed:17938955,
CC ECO:0000269|PubMed:29177846}.
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:17938955};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21890;
CC Evidence={ECO:0000269|PubMed:17938955};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:P42593};
CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:17938955}.
CC -!- INDUCTION: By wounding, jasmonate and drought stress.
CC {ECO:0000269|PubMed:17938955, ECO:0000269|PubMed:18786507}.
CC -!- DISRUPTION PHENOTYPE: Open glumes after anthesis associated with a
CC delayed cell degradation process of the lodicules (PubMed:29177846).
CC Reduced grain filling (PubMed:29177846). {ECO:0000269|PubMed:29177846}.
CC -!- MISCELLANEOUS: Over-expression of OPR7 in Arabidopsis thaliana opr3
CC mutant functionally complements the male sterility phenotype and
CC restores jasmonate production. {ECO:0000269|PubMed:17938955}.
CC -!- SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase
CC family. {ECO:0000305}.
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DR EMBL; AP004586; BAD09599.1; -; Genomic_DNA.
DR EMBL; AP004707; BAD09954.1; -; Genomic_DNA.
DR EMBL; AP008214; BAF23889.1; -; Genomic_DNA.
DR EMBL; AP014964; BAT05755.1; -; Genomic_DNA.
DR EMBL; CM000145; EAZ42984.1; -; Genomic_DNA.
DR EMBL; AK071203; BAG92371.1; -; mRNA.
DR EMBL; AK104843; BAG96990.1; -; mRNA.
DR RefSeq; XP_015650809.1; XM_015795323.1.
DR AlphaFoldDB; Q6Z965; -.
DR SMR; Q6Z965; -.
DR STRING; 4530.OS08T0459600-01; -.
DR PaxDb; Q6Z965; -.
DR PRIDE; Q6Z965; -.
DR EnsemblPlants; Os08t0459600-01; Os08t0459600-01; Os08g0459600.
DR GeneID; 4345762; -.
DR Gramene; Os08t0459600-01; Os08t0459600-01; Os08g0459600.
DR KEGG; osa:4345762; -.
DR eggNOG; KOG0134; Eukaryota.
DR HOGENOM; CLU_012153_0_2_1; -.
DR InParanoid; Q6Z965; -.
DR OMA; QPKGHVS; -.
DR OrthoDB; 978998at2759; -.
DR PlantReactome; R-OSA-1119332; Jasmonic acid biosynthesis.
DR PlantReactome; R-OSA-6787011; Jasmonic acid signaling.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000007752; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR Genevisible; Q6Z965; OS.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0016629; F:12-oxophytodienoate reductase activity; IDA:UniProtKB.
DR GO; GO:0010181; F:FMN binding; IEA:EnsemblPlants.
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:0009695; P:jasmonic acid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009620; P:response to fungus; IEA:EnsemblPlants.
DR GO; GO:0010193; P:response to ozone; IEA:EnsemblPlants.
DR GO; GO:0048443; P:stamen development; IEA:EnsemblPlants.
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; Peroxisome; Reference proteome.
FT CHAIN 1..394
FT /note="12-oxophytodienoate reductase 7"
FT /id="PRO_0000410713"
FT MOTIF 392..394
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 194
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 35..37
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 110
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 189..192
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 241
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 286
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 324
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 345..346
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P42593"
SQ SEQUENCE 394 AA; 43677 MW; CAC0A1F6D148D2E5 CRC64;
MDRPPPDQQR QKQAPLFSPY QMPRFRLNHR VVLAPMTRCR AIGGVPGPAL AEYYAQRTTQ
GGLLISEGTV VSPAGPGFPH VPGIYNQEQT DAWKKVVDAV HAKGGIFFCQ LWHVGRASHQ
VYQPNGAAPI SSTDKPISAR WRILMPDGSY GKYPKPRRLA ASEIPEIVEQ YRQAAINAIE
AGFDGIEIHG AHGYIIDQFL KDGINDRTDE YGGSLSNRCR FLLEVTRAVV SAIGADRVAV
RISPAIDHLD AYDSDPIKLG MAVVERLNAL QQQSGRLAYL HVTQPRYTAY GQTESGQHGS
AEEESRLMRT LRGTYQGTFM CSGGYTRELG LEAVESGDAD LVSYGRLFIS NPDLVERFRL
NAGLNKYVRK TFYTPDPVVG YTDYPFLGQP KSRM
