OPR2_ARATH
ID OPR2_ARATH Reviewed; 374 AA.
AC Q8GYB8; Q1LYX5; Q9ZR80;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=12-oxophytodienoate reductase 2 {ECO:0000303|PubMed:10333582};
DE EC=1.3.1.42 {ECO:0000269|PubMed:10872231};
DE AltName: Full=12-oxophytodienoate-10,11-reductase 2 {ECO:0000303|PubMed:10333582};
DE Short=AtOPR2 {ECO:0000303|PubMed:10333582};
DE Short=OPDA-reductase 2 {ECO:0000305};
DE AltName: Full=4,5-didehydrojasmonate reductase {ECO:0000303|PubMed:29291349};
DE EC=1.3.1.- {ECO:0000269|PubMed:29291349};
GN Name=OPR2 {ECO:0000303|PubMed:10333582};
GN OrderedLocusNames=At1g76690 {ECO:0000312|Araport:AT1G76690};
GN ORFNames=F28O16.6 {ECO:0000312|EMBL:AAF04449.1};
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 [GENOMIC DNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP 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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 [8]
RP INDUCTION.
RX PubMed=15923336; DOI=10.1104/pp.104.056168;
RA Mezzari M.P., Walters K., Jelinkova M., Shih M.C., Just C.L., Schnoor J.L.;
RT "Gene expression and microscopic analysis of Arabidopsis exposed to
RT chloroacetanilide herbicides and explosive compounds. A phytoremediation
RT approach.";
RL Plant Physiol. 138:858-869(2005).
RN [9]
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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=29291349; DOI=10.1038/nchembio.2540;
RA Chini A., Monte I., Zamarreno A.M., Hamberg M., Lassueur S., Reymond P.,
RA Weiss S., Stintzi A., Schaller A., Porzel A., Garcia-Mina J.M., Solano R.;
RT "An OPR3-independent pathway uses 4,5-didehydrojasmonate for jasmonate
RT synthesis.";
RL Nat. Chem. Biol. 14:171-178(2018).
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 (Probable). May be involved in the
CC biosynthesis or metabolism of oxylipin signaling molecules
CC (PubMed:10872231) (Probable). In vitro, reduces 9R,13R-12-
CC oxophytodienoic acid (9R,13R-OPDA) to 9R,13R-OPC-8:0, but only poorly
CC 9S,13S-OPDA, the natural precursor of jasmonic acid (JA)
CC (PubMed:10872231). Can detoxify the explosive 2,4,6-trinitrotoluene
CC (TNT) in vitro and in vivo by catalyzing its nitroreduction to form
CC hydroxylamino-dinitrotoluene (HADNT) (PubMed:19605548). Functions in an
CC alternative and OPR3-independent pathway for JA biosynthesis
CC (PubMed:29291349). Catalyzes the NADPH-dependent reduction of 4,5-
CC didehydrojasmonates to jasmonates (PubMed:29291349).
CC {ECO:0000269|PubMed:10872231, ECO:0000269|PubMed:19605548,
CC ECO:0000269|PubMed:29291349, ECO:0000305|PubMed:10872231}.
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};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 4,5-didehydrojasmonate + H(+) + NADPH = a jasmonate +
CC NADP(+); Xref=Rhea:RHEA:58072, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:136184, ChEBI:CHEBI:142502;
CC Evidence={ECO:0000269|PubMed:29291349};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:10872231};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=218 uM for 4,5-didehydrojasmonate {ECO:0000269|PubMed:29291349};
CC Note=kcat is 0.819 sec(-1) with 4,5-didehydrojasmonate as substrate.
CC {ECO:0000269|PubMed:29291349};
CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12445129}.
CC -!- TISSUE SPECIFICITY: Expressed at highest levels in roots and
CC cotyledons, and at lower levels in leaves, shoots and flowers (sepals,
CC petals, maturing siliques and developing pollen).
CC {ECO:0000269|PubMed:10333582}.
CC -!- DEVELOPMENTAL STAGE: Expressed during late steps of pollen development.
CC {ECO:0000269|PubMed:10333582}.
CC -!- INDUCTION: By wounding, locally and systemically, by cold and heat
CC stresses, and by UV-C. Seems to not be influenced by UV-A and UV-B.
CC Induced by the chloroacetanilide herbicides acetochlor and metolachlor,
CC and the explosives 2,4,6-trinitrotoluene (TNT) and hexahydro-1,3,5-
CC trinitro-1,3,5-triazine (RDX). {ECO:0000269|PubMed:10333582,
CC ECO:0000269|PubMed:15923336, ECO:0000269|PubMed:19605548}.
CC -!- SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase
CC family. {ECO:0000305}.
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DR EMBL; U92460; AAC78441.1; -; Genomic_DNA.
DR EMBL; AC010718; AAF04449.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35876.1; -; Genomic_DNA.
DR EMBL; AK117738; BAC42387.1; -; mRNA.
DR EMBL; BT025251; ABF19004.1; -; mRNA.
DR PIR; C96795; C96795.
DR RefSeq; NP_177795.1; NM_106319.5.
DR AlphaFoldDB; Q8GYB8; -.
DR SMR; Q8GYB8; -.
DR STRING; 3702.AT1G76690.1; -.
DR iPTMnet; Q8GYB8; -.
DR PaxDb; Q8GYB8; -.
DR PRIDE; Q8GYB8; -.
DR ProteomicsDB; 248760; -.
DR EnsemblPlants; AT1G76690.1; AT1G76690.1; AT1G76690.
DR GeneID; 844002; -.
DR Gramene; AT1G76690.1; AT1G76690.1; AT1G76690.
DR KEGG; ath:AT1G76690; -.
DR Araport; AT1G76690; -.
DR TAIR; locus:2030096; AT1G76690.
DR eggNOG; KOG0134; Eukaryota.
DR HOGENOM; CLU_012153_0_0_1; -.
DR InParanoid; Q8GYB8; -.
DR OMA; YDVIIAF; -.
DR OrthoDB; 978998at2759; -.
DR PhylomeDB; Q8GYB8; -.
DR BioCyc; ARA:AT1G76690-MON; -.
DR BRENDA; 1.3.1.42; 399.
DR UniPathway; UPA00382; -.
DR PRO; PR:Q8GYB8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8GYB8; baseline and differential.
DR Genevisible; Q8GYB8; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
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: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; IEA:UniProtKB-UniPathway.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
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 Acetylation; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW Flavoprotein; FMN; Lipid biosynthesis; Lipid metabolism; NADP;
KW Oxidoreductase; Oxylipin biosynthesis; Reference proteome.
FT CHAIN 1..374
FT /note="12-oxophytodienoate reductase 2"
FT /id="PRO_0000194484"
FT ACT_SITE 190
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9FUP0"
FT BINDING 33..35
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9FUP0"
FT BINDING 66
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9FUP0"
FT BINDING 108
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9FUP0"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9FUP0"
FT BINDING 237
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9FUP0"
FT BINDING 277
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9FUP0"
FT BINDING 305..307
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9FUP0"
FT BINDING 328..329
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:0007744|PubMed:22223895"
FT CONFLICT 174
FT /note="A -> T (in Ref. 4; BAC42387)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 374 AA; 41567 MW; 3168EDF4E857A883 CRC64;
MEMVNAEAKQ SVPLLTPYKM GRFNLSHRVV LAPLTRQKSY GSVPQPHAIL YYSQRTSPGG
FLIAEATGVS DTAQGYPDTP GIWTKEHVEA WKPIVDAVHA KGGIFFCQIW HVGRVSNRGF
QPRRQAPISC TGKPIMPQMR ANGIDEARFT PPRRLSIEEI PGIVNDFRLA ARNAMEAGFD
GVEIHGAHGY LIDQFMKDKV NDRTDEYGGS LQNRCKFALE VVDAVAKEIG PDRVGIRLSP
FADYMESGDT NPEALGLYMV ESLNKYGILY CHMIEPRMKT VGEIAACSHT LMPMREAFKG
TFISAGGFTR EDGNEAVAKG RTDLVAYGRW FLANPDLPKR FQLDAPLNKY NRSTFYTSDP
VVGYTDYPSL ESTA
