ID   OPRL_SOLLC              Reviewed;         355 AA.
AC   Q9FEX0;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=12-oxophytodienoate reductase-like protein;
DE            EC=1.3.1.-;
DE   AltName: Full=LeOPR2;
GN   Name=OPR2;
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], TISSUE SPECIFICITY, AND 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).
CC   -!- FUNCTION: May be involved in the biosynthesis or metabolism of oxylipin
CC       signaling molecules. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12445129}.
CC   -!- TISSUE SPECIFICITY: Weakly expressed in flowers and roots.
CC       {ECO:0000269|PubMed:12445129}.
CC   -!- INDUCTION: Seems to not be influenced by wounding.
CC   -!- SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase
CC       family. {ECO:0000305}.
CC   -!- CAUTION: Was named OAX2 but it does correspond to Arabidopsis OAX2
CC       protein. {ECO:0000305}.
CC   -!- CAUTION: According to PubMed:12445129, no association with a flavin
CC       cofactor is detected. Does not reduce 12-oxophytodienoic acid (OPDA)
CC       nor any other alpha,beta-unsaturated carbonyl tested. {ECO:0000305}.
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DR   EMBL; AJ278331; CAC21423.1; -; mRNA.
DR   RefSeq; NP_001233868.2; NM_001246939.3.
DR   AlphaFoldDB; Q9FEX0; -.
DR   SMR; Q9FEX0; -.
DR   STRING; 4081.Solyc01g103390.2.1; -.
DR   PaxDb; Q9FEX0; -.
DR   PRIDE; Q9FEX0; -.
DR   GeneID; 543762; -.
DR   KEGG; sly:543762; -.
DR   eggNOG; KOG0134; Eukaryota.
DR   InParanoid; Q9FEX0; -.
DR   OrthoDB; 978998at2759; -.
DR   BRENDA; 1.3.1.42; 3101.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; Q9FEX0; baseline.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Cytoplasm; Flavoprotein; FMN; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..355
FT                   /note="12-oxophytodienoate reductase-like protein"
FT                   /id="PRO_0000194490"
FT   ACT_SITE        181
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         30..32
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         63
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         175..178
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         265
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         288
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         309..310
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   355 AA;  39342 MW;  F4A52780C069EAA0 CRC64;
     MEANSNSAVP LCTPYKLGRF KLTHRIVFPA LTRNRSQNNT PQSHLTEYYS QRATNGGLII
     SEAAAASDIS KECPNLPGIW NEEQVEAWKP VVNGVHEKGG VFFCQIWHSG RLSVPTVSAL
     FFSIGIGWST RPDDKVYAKP TPLPLESDKI PCIVNDFRIA ARNAIKAGFD GIEINASSGG
     YLIDEFMNDQ VHGWTDEYDE SIKDRCRLAL EIVEAVANEI GADKIGIKLS PFDGKKDSNS
     EALATYMANE LSKLGVLYLH VMEPRETVNR SLLPIRKAFK GTLIASGGYG KSDGEKAIDE
     NYADLISFGR MFLANPDLPK RFEVNAPLNK YNRSTFYTND PIIGYTDYPF LEVAS