OPR1_ARATH
ID OPR1_ARATH Reviewed; 372 AA.
AC Q8LAH7; O49259; Q9S806;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=12-oxophytodienoate reductase 1 {ECO:0000303|PubMed:10333582};
DE EC=1.3.1.42 {ECO:0000269|PubMed:10872231, ECO:0000269|PubMed:9346960};
DE AltName: Full=12-oxophytodienoate-10,11-reductase 1 {ECO:0000303|PubMed:10333582};
DE Short=AtOPR1 {ECO:0000303|PubMed:10333582};
DE Short=OPDA-reductase 1 {ECO:0000305};
DE AltName: Full=FS-AT-I {ECO:0000305};
GN Name=OPR1 {ECO:0000303|PubMed:10333582};
GN OrderedLocusNames=At1g76680 {ECO:0000312|Araport:AT1G76680};
GN ORFNames=F28O16.5 {ECO:0000312|EMBL:AAF04448.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia;
RX PubMed=9346960; DOI=10.1074/jbc.272.44.28066;
RA Schaller F., Weiler E.W.;
RT "Molecular cloning and characterization of 12-oxophytodienoate reductase,
RT an enzyme of the octadecanoid signaling pathway from Arabidopsis thaliana.
RT Structural and functional relationship to yeast old yellow enzyme.";
RL J. Biol. Chem. 272:28066-28072(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=10333582; DOI=10.1007/s004250050545;
RA Biesgen C., Weiler E.W.;
RT "Structure and regulation of OPR1 and OPR2, two closely related genes
RT encoding 12-oxophytodienoic acid-10,11-reductases from Arabidopsis
RT thaliana.";
RL Planta 208:155-165(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND COFACTOR.
RX PubMed=10872231; DOI=10.1007/s004250050706;
RA Schaller F., Biesgen C., Muessig C., Altmann T., Weiler E.W.;
RT "12-Oxophytodienoate reductase 3 (OPR3) is the isoenzyme involved in
RT jasmonate biosynthesis.";
RL Planta 210:979-984(2000).
RN [9]
RP INDUCTION.
RX PubMed=11725945; DOI=10.1023/a:1012211011538;
RA He Y., Gan S.;
RT "Identical promoter elements are involved in regulation of the OPR1 gene by
RT senescence and jasmonic acid in Arabidopsis.";
RL Plant Mol. Biol. 47:595-605(2001).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=12445129; DOI=10.1046/j.1365-313x.2002.01449.x;
RA Strassner J., Schaller F., Frick U.B., Howe G.A., Weiler E.W., Amrhein N.,
RA Macheroux P., Schaller A.;
RT "Characterization and cDNA-microarray expression analysis of 12-
RT oxophytodienoate reductases reveals differential roles for octadecanoid
RT biosynthesis in the local versus the systemic wound response.";
RL Plant J. 32:585-601(2002).
RN [11]
RP FUNCTION, AND INDUCTION.
RX PubMed=19605548; DOI=10.1104/pp.109.141598;
RA Beynon E.R., Symons Z.C., Jackson R.G., Lorenz A., Rylott E.L., Bruce N.C.;
RT "The role of oxophytodienoate reductases in the detoxification of the
RT explosive 2,4,6-trinitrotoluene by Arabidopsis.";
RL Plant Physiol. 151:253-261(2009).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH FMN, AND COFACTOR.
RX PubMed=16080145; DOI=10.1002/prot.20533;
RA Fox B.G., Malone T.E., Johnson K.A., Madson S.E., Aceti D., Bingman C.A.,
RA Blommel P.G., Buchan B., Burns B., Cao J., Cornilescu C., Doreleijers J.,
RA Ellefson J., Frederick R., Geetha H., Hruby D., Jeon W.B., Kimball T.,
RA Kunert J., Markley J.L., Newman C., Olson A., Peterson F.C.,
RA Phillips G.N. Jr., Primm J., Ramirez B., Rosenberg N.S., Runnels M.,
RA Seder K., Shaw J., Smith D.W., Sreenath H., Song J., Sussman M.R., Thao S.,
RA Troestler D., Tyler E., Tyler R., Ulrich E., Vinarov D., Vojtik F.,
RA Volkman B.F., Wesenberg G., Wrobel R.L., Zhang J., Zhao Q., Zolnai Z.;
RT "X-ray structure of Arabidopsis At1g77680, 12-oxophytodienoate reductase
RT isoform 1.";
RL Proteins 61:206-208(2005).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH FMN.
RX PubMed=17850744; DOI=10.1016/j.str.2007.06.019;
RA Levin E.J., Kondrashov D.A., Wesenberg G.E., Phillips G.N. Jr.;
RT "Ensemble refinement of protein crystal structures: validation and
RT application.";
RL Structure 15:1040-1052(2007).
CC -!- FUNCTION: Specifically cleaves olefinic bonds in alpha,beta-unsaturated
CC carbonyls and may be involved in detoxification or modification of
CC these reactive compounds (PubMed:9346960, PubMed:10872231). May be
CC involved in the biosynthesis or metabolism of oxylipin signaling
CC molecules (Probable). In vitro, reduces 9R,13R-12-oxophytodienoic acid
CC (9R,13R-OPDA) to 9R,13R-OPC-8:0, but only poorly 9S,13S-OPDA, the
CC natural precursor of jasmonic acid (PubMed:10872231). Can detoxify the
CC explosive 2,4,6-trinitrotoluene (TNT) in vitro and in vivo by
CC catalyzing its nitroreduction to form hydroxylamino-dinitrotoluene
CC (HADNT) (PubMed:19605548). {ECO:0000269|PubMed:10872231,
CC ECO:0000269|PubMed:19605548, ECO:0000269|PubMed:9346960,
CC ECO:0000305|PubMed:9346960}.
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:10872231, ECO:0000269|PubMed:9346960};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:10872231};
CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000305}.
CC -!- INTERACTION:
CC Q8LAH7; A0A384KC16: At3g63260; NbExp=3; IntAct=EBI-2926709, EBI-25521837;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12445129}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=Q8LAH7-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots, also present in leaves,
CC shoots and flowers. More abundant in cotyledons. In more details,
CC expressed in peduncles, sepals, petals, around the abscission zone of
CC siliques, maturing siliques and developing seeds.
CC {ECO:0000269|PubMed:10333582}.
CC -!- DEVELOPMENTAL STAGE: Expressed during leaves senescence, seeds
CC development, and siliques maturation.
CC -!- INDUCTION: By wounding, locally and systemically, by cold and heat
CC stresses, by jasmonate and by UV-C. Up-regulated during senescence.
CC Seems to not be influenced by UV-A and UV-B. Induced by the explosive
CC 2,4,6-trinitrotoluene (TNT). {ECO:0000269|PubMed:10333582,
CC ECO:0000269|PubMed:11725945, ECO:0000269|PubMed:19605548}.
CC -!- SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase
CC family. {ECO:0000305}.
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DR EMBL; Y10617; CAA71627.1; -; mRNA.
DR EMBL; U92460; AAC78440.1; -; Genomic_DNA.
DR EMBL; AC010718; AAF04448.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35875.1; -; Genomic_DNA.
DR EMBL; AY074874; AAL75894.1; -; mRNA.
DR EMBL; BT020365; AAV85720.1; -; mRNA.
DR EMBL; AY087801; AAM65337.1; -; mRNA.
DR PIR; B96795; B96795.
DR RefSeq; NP_177794.1; NM_106318.4. [Q8LAH7-1]
DR PDB; 1VJI; X-ray; 2.00 A; A=1-372.
DR PDB; 2Q3R; X-ray; 2.00 A; A=1-372.
DR PDBsum; 1VJI; -.
DR PDBsum; 2Q3R; -.
DR AlphaFoldDB; Q8LAH7; -.
DR SMR; Q8LAH7; -.
DR BioGRID; 29220; 1.
DR IntAct; Q8LAH7; 2.
DR STRING; 3702.AT1G76680.2; -.
DR PRIDE; Q8LAH7; -.
DR ProteomicsDB; 249368; -. [Q8LAH7-1]
DR EnsemblPlants; AT1G76680.1; AT1G76680.1; AT1G76680. [Q8LAH7-1]
DR GeneID; 844001; -.
DR Gramene; AT1G76680.1; AT1G76680.1; AT1G76680. [Q8LAH7-1]
DR KEGG; ath:AT1G76680; -.
DR Araport; AT1G76680; -.
DR eggNOG; KOG0134; Eukaryota.
DR HOGENOM; CLU_012153_0_0_1; -.
DR InParanoid; Q8LAH7; -.
DR PhylomeDB; Q8LAH7; -.
DR BioCyc; ARA:AT1G76680-MON; -.
DR BRENDA; 1.3.1.42; 399.
DR UniPathway; UPA00382; -.
DR EvolutionaryTrace; Q8LAH7; -.
DR PRO; PR:Q8LAH7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8LAH7; baseline and differential.
DR Genevisible; Q8LAH7; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016629; F:12-oxophytodienoate reductase activity; IDA:UniProtKB.
DR GO; GO:0010181; F:FMN binding; IDA:UniProtKB.
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-UniPathway.
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 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Fatty acid biosynthesis; Fatty acid metabolism; Flavoprotein; FMN;
KW Lipid biosynthesis; Lipid metabolism; NADP; Oxidoreductase;
KW Oxylipin biosynthesis; Reference proteome.
FT CHAIN 1..372
FT /note="12-oxophytodienoate reductase 1"
FT /id="PRO_0000194483"
FT ACT_SITE 188
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9FUP0"
FT BINDING 31..33
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16080145,
FT ECO:0000269|PubMed:17850744, ECO:0007744|PDB:1VJI,
FT ECO:0007744|PDB:2Q3R"
FT BINDING 64
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16080145,
FT ECO:0000269|PubMed:17850744, ECO:0007744|PDB:1VJI,
FT ECO:0007744|PDB:2Q3R"
FT BINDING 106
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16080145,
FT ECO:0000269|PubMed:17850744, ECO:0007744|PDB:1VJI,
FT ECO:0007744|PDB:2Q3R"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9FUP0"
FT BINDING 235
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16080145,
FT ECO:0000269|PubMed:17850744, ECO:0007744|PDB:1VJI,
FT ECO:0007744|PDB:2Q3R"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9FUP0"
FT BINDING 303..305
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16080145,
FT ECO:0000269|PubMed:17850744, ECO:0007744|PDB:1VJI,
FT ECO:0007744|PDB:2Q3R"
FT BINDING 326..327
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9FUP0"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8GYB8"
FT CONFLICT 43..44
FT /note="Missing (in Ref. 1; CAA71627)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="G -> R (in Ref. 7; AAM65337)"
FT /evidence="ECO:0000305"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:2Q3R"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:2Q3R"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:2Q3R"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:2Q3R"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:2Q3R"
FT HELIX 44..52
FT /evidence="ECO:0007829|PDB:2Q3R"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:2Q3R"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:2Q3R"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:2Q3R"
FT HELIX 83..97
FT /evidence="ECO:0007829|PDB:2Q3R"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:2Q3R"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:2Q3R"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:2Q3R"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:2Q3R"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:2Q3R"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:2Q3R"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:2Q3R"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:2Q3R"
FT HELIX 158..175
FT /evidence="ECO:0007829|PDB:2Q3R"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:2Q3R"
FT HELIX 189..194
FT /evidence="ECO:0007829|PDB:2Q3R"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:2Q3R"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:2Q3R"
FT HELIX 209..227
FT /evidence="ECO:0007829|PDB:2Q3R"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:2Q3R"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:2Q3R"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:2Q3R"
FT HELIX 250..264
FT /evidence="ECO:0007829|PDB:2Q3R"
FT STRAND 267..272
FT /evidence="ECO:0007829|PDB:2Q3R"
FT HELIX 290..295
FT /evidence="ECO:0007829|PDB:2Q3R"
FT STRAND 297..305
FT /evidence="ECO:0007829|PDB:2Q3R"
FT HELIX 309..316
FT /evidence="ECO:0007829|PDB:2Q3R"
FT STRAND 321..326
FT /evidence="ECO:0007829|PDB:2Q3R"
FT HELIX 327..330
FT /evidence="ECO:0007829|PDB:2Q3R"
FT HELIX 335..338
FT /evidence="ECO:0007829|PDB:2Q3R"
FT HELIX 350..353
FT /evidence="ECO:0007829|PDB:2Q3R"
FT TURN 360..362
FT /evidence="ECO:0007829|PDB:2Q3R"
SQ SEQUENCE 372 AA; 41168 MW; 213C8C850FF691CB CRC64;
MENGEAKQSV PLLTPYKMGR FNLSHRVVLA PLTRQRSYGN VPQPHAAIYY SQRTTPGGFL
ITEATGVSDT AQGYQDTPGI WTKEHVEAWK PIVDAVHAKG GIFFCQIWHV GRVSNSGFQP
NGKAPISCSD KPLMPQIRSN GIDEALFTPP RRLGIEEIPG IVNDFRLAAR NAMEAGFDGV
EIHGANGYLI DQFMKDTVND RTDEYGGSLQ NRCKFPLEIV DAVAKEIGPD RVGIRLSPFA
DYMESGDTNP GALGLYMAES LNKYGILYCH VIEARMKTMG EVHACPHTLM PMRKAFKGTF
ISAGGFTRED GNEAVSKGRT DLVAYGRWFL ANPDLPKRFQ VDAPLNKYDR PTFYTSDPVV
GYTDYPFLES TA
