OPR1_SOLLC
ID OPR1_SOLLC Reviewed; 376 AA.
AC Q9XG54;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=12-oxophytodienoate reductase 1;
DE EC=1.3.1.42;
DE AltName: Full=12-oxophytodienoate-10,11-reductase 1;
DE Short=OPDA-reductase 1;
DE AltName: Full=LeOPR1;
GN Name=OPR1;
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 CATALYTIC ACTIVITY.
RC STRAIN=cv. Castlemart II; TISSUE=Shoot;
RX PubMed=10574986; DOI=10.1074/jbc.274.49.35067;
RA Strassner J., Fuerholz A., Macheroux P., Amrhein N., Schaller A.;
RT "A homolog of old yellow enzyme in tomato: spectral properties and
RT substrate specificity of the recombinant protein.";
RL J. Biol. Chem. 274:35067-35073(1999).
RN [2]
RP FUNCTION, COFACTOR, SUBSTRATE 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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, SUBSTRATE
RP SPECIFICITY, AND COFACTOR-BINDING.
RX PubMed=11377202; DOI=10.1016/s0969-2126(01)00602-5;
RA Breithaupt C., Strassner J., Breitinger U., Huber R., Macheroux P.,
RA Schaller A., Clausen T.;
RT "X-ray structure of 12-oxophytodienoate reductase 1 provides structural
RT insight into substrate binding and specificity within the family of OYE.";
RL Structure 9:419-429(2001).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.30 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 alpha,beta-unsaturated
CC carbonyls and may be involved in detoxification or modification of
CC these reactive compounds. May be involved in the biosynthesis or
CC metabolism of oxylipin signaling molecules. In vitro, reduces 9R,13R-
CC 12-oxophyodienoic acid (9R,13R-OPDA) to 9R,13R-OPC-8:0, but not 9S,13S-
CC OPDA, the natural precursor of jasmonic acid. Also reduces N-
CC ethylmaleimide and maleic acid. {ECO:0000269|PubMed:12445129}.
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:10574986};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:11377202, ECO:0000269|PubMed:12445129};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8 uM for N-ethylmaleimide (at pH 7.0 and 25 degrees Celsius);
CC KM=47 uM for maleic acid (at pH 7.0 and 25 degrees Celsius);
CC KM=15 uM for OPDA (at pH 7.0 and 25 degrees Celsius);
CC Note=The highest catalytic efficiency was observed with N-
CC ethylmaleimide.;
CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12445129}.
CC -!- TISSUE SPECIFICITY: Constitutively expressed in roots, leaves,
CC cotyledons, cells culture and to a lower extent in flowers.
CC {ECO:0000269|PubMed:10574986}.
CC -!- INDUCTION: Seems to not be influenced by wounding.
CC -!- SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase
CC family. {ECO:0000305}.
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DR EMBL; AJ242551; CAB43506.1; -; mRNA.
DR RefSeq; NP_001234781.1; NM_001247852.1.
DR PDB; 1ICP; X-ray; 1.90 A; A/B=1-376.
DR PDB; 1ICQ; X-ray; 2.00 A; A/B=1-376.
DR PDB; 1ICS; X-ray; 2.30 A; A/B=1-376.
DR PDB; 3HGR; X-ray; 2.30 A; A/B=1-376.
DR PDBsum; 1ICP; -.
DR PDBsum; 1ICQ; -.
DR PDBsum; 1ICS; -.
DR PDBsum; 3HGR; -.
DR AlphaFoldDB; Q9XG54; -.
DR SMR; Q9XG54; -.
DR STRING; 4081.Solyc10g086220.1.1; -.
DR PaxDb; Q9XG54; -.
DR PRIDE; Q9XG54; -.
DR EnsemblPlants; Solyc10g086220.2.1; Solyc10g086220.2.1; Solyc10g086220.2.
DR GeneID; 544239; -.
DR Gramene; Solyc10g086220.2.1; Solyc10g086220.2.1; Solyc10g086220.2.
DR KEGG; sly:544239; -.
DR eggNOG; KOG0134; Eukaryota.
DR HOGENOM; CLU_012153_0_0_1; -.
DR InParanoid; Q9XG54; -.
DR OMA; YQDTPGL; -.
DR OrthoDB; 978998at2759; -.
DR PhylomeDB; Q9XG54; -.
DR BRENDA; 1.3.1.42; 3101.
DR UniPathway; UPA00382; -.
DR EvolutionaryTrace; Q9XG54; -.
DR Proteomes; UP000004994; Chromosome 10.
DR ExpressionAtlas; Q9XG54; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016629; F:12-oxophytodienoate reductase activity; IEA:UniProtKB-EC.
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: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; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW Flavoprotein; FMN; Lipid biosynthesis; Lipid metabolism; NADP;
KW Oxidoreductase; Oxylipin biosynthesis; Reference proteome.
FT CHAIN 1..376
FT /note="12-oxophytodienoate reductase 1"
FT /id="PRO_0000194488"
FT ACT_SITE 192
FT /note="Proton donor"
FT BINDING 35..37
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:19660473"
FT BINDING 68
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:19660473"
FT BINDING 110
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:19660473"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11377202"
FT BINDING 187..190
FT /ligand="substrate"
FT BINDING 239
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:19660473"
FT BINDING 279
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 309
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:19660473"
FT BINDING 330..331
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:19660473"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:1ICP"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:1ICP"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:1ICP"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:1ICP"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:1ICP"
FT HELIX 48..56
FT /evidence="ECO:0007829|PDB:1ICP"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:1ICP"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:1ICQ"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:1ICP"
FT HELIX 87..102
FT /evidence="ECO:0007829|PDB:1ICP"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:1ICP"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:1ICP"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:1ICP"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:1ICP"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:1ICQ"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:1ICP"
FT HELIX 162..178
FT /evidence="ECO:0007829|PDB:1ICP"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:1ICP"
FT HELIX 193..198
FT /evidence="ECO:0007829|PDB:1ICP"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:1ICP"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:1ICP"
FT HELIX 213..231
FT /evidence="ECO:0007829|PDB:1ICP"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:1ICP"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:1ICP"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:1ICP"
FT HELIX 254..265
FT /evidence="ECO:0007829|PDB:1ICP"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:1ICP"
FT STRAND 271..276
FT /evidence="ECO:0007829|PDB:1ICP"
FT HELIX 294..299
FT /evidence="ECO:0007829|PDB:1ICP"
FT STRAND 304..309
FT /evidence="ECO:0007829|PDB:1ICP"
FT HELIX 312..320
FT /evidence="ECO:0007829|PDB:1ICP"
FT STRAND 325..330
FT /evidence="ECO:0007829|PDB:1ICP"
FT HELIX 331..335
FT /evidence="ECO:0007829|PDB:1ICP"
FT HELIX 339..345
FT /evidence="ECO:0007829|PDB:1ICP"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:1ICP"
FT TURN 364..366
FT /evidence="ECO:0007829|PDB:1ICP"
SQ SEQUENCE 376 AA; 42415 MW; 83CFBEAC7CBC7A8F CRC64;
MENKVVEEKQ VDKIPLMSPC KMGKFELCHR VVLAPLTRQR SYGYIPQPHA ILHYSQRSTN
GGLLIGEATV ISETGIGYKD VPGIWTKEQV EAWKPIVDAV HAKGGIFFCQ IWHVGRVSNK
DFQPNGEDPI SCTDRGLTPQ IRSNGIDIAH FTRPRRLTTD EIPQIVNEFR VAARNAIEAG
FDGVEIHGAH GYLIDQFMKD QVNDRSDKYG GSLENRCRFA LEIVEAVANE IGSDRVGIRI
SPFAHYNEAG DTNPTALGLY MVESLNKYDL AYCHVVEPRM KTAWEKIECT ESLVPMRKAY
KGTFIVAGGY DREDGNRALI EDRADLVAYG RLFISNPDLP KRFELNAPLN KYNRDTFYTS
DPIVGYTDYP FLETMT
