OPR3_SOLLC
ID OPR3_SOLLC Reviewed; 396 AA.
AC Q9FEW9;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=12-oxophytodienoate reductase 3;
DE EC=1.3.1.42;
DE AltName: Full=12-oxophytodienoate-10,11-reductase 3;
DE Short=OPDA-reductase 3;
DE AltName: Full=LeOPR3;
GN Name=OPR3;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], COFACTOR, SUBSTRATE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Castlemart II; TISSUE=Shoot;
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 [2]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH FMN.
RX PubMed=16983071; DOI=10.1073/pnas.0606603103;
RA Breithaupt C., Kurzbauer R., Lilie H., Schaller A., Strassner J., Huber R.,
RA Macheroux P., Clausen T.;
RT "Crystal structure of 12-oxophytodienoate reductase 3 from tomato: self-
RT inhibition by dimerization.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:14337-14342(2006).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH FMN.
RX PubMed=19660473; DOI=10.1016/j.jmb.2009.07.087;
RA Breithaupt C., Kurzbauer R., Schaller F., Stintzi A., Schaller A.,
RA Huber R., Macheroux P., Clausen T.;
RT "Structural basis of substrate specificity of plant 12-oxophytodienoate
RT reductases.";
RL J. Mol. Biol. 392:1266-1277(2009).
CC -!- FUNCTION: Specifically cleaves olefinic bonds in cyclic enones.
CC Involved in the biosynthesis of jasmonic acid (JA) and perhaps in
CC biosynthesis or metabolism of other oxylipin signaling moleclules. It
CC is required for the spatial and temporal regulation of JA levels during
CC dehiscence of anthers, promoting the stomium degeneration program (By
CC similarity). In vitro, reduces 9S,13S-12-oxophytodienoic acid (9S,13S-
CC OPDA) and 9R,13R-OPDA to 9S,13S-OPC-8:0 and 9R,13R-OPC-8:0,
CC respectively. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis.
CC -!- INTERACTION:
CC Q9FEW9; Q9FEW9: OPR3; NbExp=4; IntAct=EBI-15601730, EBI-15601730;
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:12445129}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and to a lower extent in leaves
CC and flowers.
CC -!- INDUCTION: By wounding, locally and systemically.
CC -!- SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ278332; CAC21424.1; -; mRNA.
DR RefSeq; NP_001233873.1; NM_001246944.2.
DR PDB; 2HS6; X-ray; 1.90 A; A/B=1-396.
DR PDB; 2HS8; X-ray; 1.90 A; A/B=1-396.
DR PDB; 2HSA; X-ray; 1.50 A; A/B=1-396.
DR PDB; 3HGO; X-ray; 2.30 A; A/B=1-396.
DR PDB; 3HGS; X-ray; 2.00 A; A/B=1-396.
DR PDBsum; 2HS6; -.
DR PDBsum; 2HS8; -.
DR PDBsum; 2HSA; -.
DR PDBsum; 3HGO; -.
DR PDBsum; 3HGS; -.
DR AlphaFoldDB; Q9FEW9; -.
DR SMR; Q9FEW9; -.
DR DIP; DIP-61271N; -.
DR STRING; 4081.Solyc07g007870.2.1; -.
DR PaxDb; Q9FEW9; -.
DR PRIDE; Q9FEW9; -.
DR EnsemblPlants; Solyc07g007870.3.1; Solyc07g007870.3.1; Solyc07g007870.3.
DR GeneID; 543763; -.
DR Gramene; Solyc07g007870.3.1; Solyc07g007870.3.1; Solyc07g007870.3.
DR KEGG; sly:543763; -.
DR eggNOG; KOG0134; Eukaryota.
DR HOGENOM; CLU_012153_0_2_1; -.
DR InParanoid; Q9FEW9; -.
DR OMA; QPKGHVS; -.
DR OrthoDB; 978998at2759; -.
DR PhylomeDB; Q9FEW9; -.
DR BRENDA; 1.3.1.42; 3101.
DR UniPathway; UPA00382; -.
DR EvolutionaryTrace; Q9FEW9; -.
DR Proteomes; UP000004994; Chromosome 7.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0016629; F:12-oxophytodienoate reductase activity; IBA:GO_Central.
DR GO; GO:0010181; F:FMN binding; IEA:EnsemblPlants.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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; IBA:GO_Central.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IBA:GO_Central.
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 3D-structure; Fatty acid biosynthesis; Fatty acid metabolism; Flavoprotein;
KW FMN; Lipid biosynthesis; Lipid metabolism; NADP; Oxidoreductase;
KW Oxylipin biosynthesis; Peroxisome; Reference proteome.
FT CHAIN 1..396
FT /note="12-oxophytodienoate reductase 3"
FT /id="PRO_0000194489"
FT REGION 342..343
FT /note="FMN"
FT MOTIF 394..396
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 190
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 31..33
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16983071,
FT ECO:0000269|PubMed:19660473"
FT BINDING 64
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16983071,
FT ECO:0000269|PubMed:19660473"
FT BINDING 106
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16983071,
FT ECO:0000269|PubMed:19660473"
FT BINDING 185..188
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 237
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16983071,
FT ECO:0000269|PubMed:19660473"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 321
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16983071,
FT ECO:0000269|PubMed:19660473"
FT BINDING 342..343
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:2HS6"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:2HSA"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:2HSA"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:2HSA"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:2HSA"
FT HELIX 44..53
FT /evidence="ECO:0007829|PDB:2HSA"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:2HSA"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:2HSA"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:2HS8"
FT HELIX 83..98
FT /evidence="ECO:0007829|PDB:2HSA"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:2HSA"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:2HSA"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:2HS6"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:2HSA"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:2HSA"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:2HSA"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:2HSA"
FT HELIX 160..176
FT /evidence="ECO:0007829|PDB:2HSA"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:2HSA"
FT HELIX 191..196
FT /evidence="ECO:0007829|PDB:2HSA"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:2HSA"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:2HSA"
FT HELIX 211..229
FT /evidence="ECO:0007829|PDB:2HSA"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:2HSA"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:2HSA"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:2HS6"
FT HELIX 252..270
FT /evidence="ECO:0007829|PDB:2HSA"
FT STRAND 275..280
FT /evidence="ECO:0007829|PDB:2HSA"
FT TURN 286..289
FT /evidence="ECO:0007829|PDB:2HSA"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:2HSA"
FT TURN 293..296
FT /evidence="ECO:0007829|PDB:2HSA"
FT HELIX 297..311
FT /evidence="ECO:0007829|PDB:2HSA"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:3HGS"
FT STRAND 316..321
FT /evidence="ECO:0007829|PDB:2HSA"
FT HELIX 324..332
FT /evidence="ECO:0007829|PDB:2HSA"
FT STRAND 337..342
FT /evidence="ECO:0007829|PDB:2HSA"
FT HELIX 343..347
FT /evidence="ECO:0007829|PDB:2HSA"
FT HELIX 351..357
FT /evidence="ECO:0007829|PDB:2HSA"
FT HELIX 366..368
FT /evidence="ECO:0007829|PDB:2HSA"
FT TURN 376..378
FT /evidence="ECO:0007829|PDB:2HSA"
SQ SEQUENCE 396 AA; 43520 MW; C9550E54D2EAF75B CRC64;
MASSAQDGNN PLFSPYKMGK FNLSHRVVLA PMTRCRALNN IPQAALGEYY EQRATAGGFL
ITEGTMISPT SAGFPHVPGI FTKEQVREWK KIVDVVHAKG AVIFCQLWHV GRASHEVYQP
AGAAPISSTE KPISNRWRIL MPDGTHGIYP KPRAIGTYEI SQVVEDYRRS ALNAIEAGFD
GIEIHGAHGY LIDQFLKDGI NDRTDEYGGS LANRCKFITQ VVQAVVSAIG ADRVGVRVSP
AIDHLDAMDS NPLSLGLAVV ERLNKIQLHS GSKLAYLHVT QPRYVAYGQT EAGRLGSEEE
EARLMRTLRN AYQGTFICSG GYTRELGIEA VAQGDADLVS YGRLFISNPD LVMRIKLNAP
LNKYNRKTFY TQDPVVGYTD YPFLQGNGSN GPLSRL
