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Protein

12-oxophytodienoate reductase 1

Gene

OPR1

Organism
Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Specifically cleaves olefinic bonds in alpha,beta-unsaturated carbonyls and may be involved in detoxification or modification of these reactive compounds. May be involved in the biosynthesis or metabolism of oxylipin signaling molecules. In vitro, reduces 9R,13R-12-oxophyodienoic acid (9R,13R-OPDA) to 9R,13R-OPC-8:0, but not 9S,13S-OPDA, the natural precursor of jasmonic acid. Also reduces N-ethylmaleimide and maleic acid.1 Publication

Catalytic activityi

8-((1R,2R)-3-oxo-2-((Z)-pent-2-enyl)cyclopentyl)octanoate + NADP+ = (15Z)-12-oxophyto-10,15-dienoate + NADPH.1 Publication

Cofactori

FMN2 Publications

Kineticsi

The highest catalytic efficiency was observed with N-ethylmaleimide.

  1. KM=8 µM for N-ethylmaleimide (at pH 7.0 and 25 degrees Celsius)
  2. KM=47 µM for maleic acid (at pH 7.0 and 25 degrees Celsius)
  3. KM=15 µM for OPDA (at pH 7.0 and 25 degrees Celsius)

    Pathwayi: oxylipin biosynthesis

    This protein is involved in the pathway oxylipin biosynthesis, which is part of Lipid metabolism.
    View all proteins of this organism that are known to be involved in the pathway oxylipin biosynthesis and in Lipid metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei68 – 681FMN; via amide nitrogen1 Publication
    Binding sitei110 – 1101FMN1 Publication
    Binding sitei143 – 1431Substrate1 Publication
    Active sitei192 – 1921Proton donor
    Binding sitei239 – 2391FMN1 Publication
    Binding sitei279 – 2791Substrate; via amide nitrogenBy similarity
    Binding sitei309 – 3091FMN; via amide nitrogen1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi35 – 373FMN1 Publication
    Nucleotide bindingi330 – 3312FMN1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Oxylipin biosynthesis

    Keywords - Ligandi

    Flavoprotein, FMN, NADP

    Enzyme and pathway databases

    BRENDAi1.3.1.42. 3101.
    UniPathwayiUPA00382.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    12-oxophytodienoate reductase 1 (EC:1.3.1.42)
    Alternative name(s):
    12-oxophytodienoate-10,11-reductase 1
    Short name:
    OPDA-reductase 1
    LeOPR1
    Gene namesi
    Name:OPR1
    OrganismiSolanum lycopersicum (Tomato) (Lycopersicon esculentum)
    Taxonomic identifieri4081 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanumLycopersicon
    Proteomesi
    • UP000004994 Componenti: Chromosome 10

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 37637612-oxophytodienoate reductase 1PRO_0000194488Add
    BLAST

    Proteomic databases

    PaxDbiQ9XG54.

    Expressioni

    Tissue specificityi

    Constitutively expressed in roots, leaves, cotyledons, cells culture and to lower extend in flowers.1 Publication

    Inductioni

    Seems to not be influenced by wounding.

    Interactioni

    Protein-protein interaction databases

    STRINGi4081.Solyc10g086220.1.1.

    Structurei

    Secondary structure

    1
    376
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi15 – 173Combined sources
    Beta strandi20 – 223Combined sources
    Beta strandi25 – 284Combined sources
    Beta strandi30 – 334Combined sources
    Helixi42 – 443Combined sources
    Helixi48 – 569Combined sources
    Beta strandi63 – 653Combined sources
    Beta strandi69 – 724Combined sources
    Helixi73 – 753Combined sources
    Helixi87 – 10216Combined sources
    Beta strandi106 – 1127Combined sources
    Turni120 – 1223Combined sources
    Helixi124 – 1263Combined sources
    Beta strandi130 – 1345Combined sources
    Beta strandi145 – 1495Combined sources
    Turni159 – 1613Combined sources
    Helixi162 – 17817Combined sources
    Beta strandi182 – 1887Combined sources
    Helixi193 – 1986Combined sources
    Turni200 – 2023Combined sources
    Beta strandi210 – 2123Combined sources
    Helixi213 – 23119Combined sources
    Helixi233 – 2353Combined sources
    Beta strandi236 – 2405Combined sources
    Turni246 – 2483Combined sources
    Helixi254 – 26512Combined sources
    Helixi266 – 2683Combined sources
    Beta strandi271 – 2766Combined sources
    Helixi294 – 2996Combined sources
    Beta strandi304 – 3096Combined sources
    Helixi312 – 3209Combined sources
    Beta strandi325 – 3306Combined sources
    Helixi331 – 3355Combined sources
    Helixi339 – 3457Combined sources
    Helixi354 – 3563Combined sources
    Turni364 – 3663Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ICPX-ray1.90A/B1-376[»]
    1ICQX-ray2.00A/B1-376[»]
    1ICSX-ray2.30A/B1-376[»]
    3HGRX-ray2.30A/B1-376[»]
    ProteinModelPortaliQ9XG54.
    SMRiQ9XG54. Positions 10-373.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9XG54.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni187 – 1904Substrate-binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiKOG0134. Eukaryota.
    COG1902. LUCA.
    InParanoidiQ9XG54.
    KOiK05894.
    OMAiECTESLV.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR001155. OxRdtase_FMN_N.
    [Graphical view]
    PfamiPF00724. Oxidored_FMN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9XG54-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MENKVVEEKQ VDKIPLMSPC KMGKFELCHR VVLAPLTRQR SYGYIPQPHA
    60 70 80 90 100
    ILHYSQRSTN GGLLIGEATV ISETGIGYKD VPGIWTKEQV EAWKPIVDAV
    110 120 130 140 150
    HAKGGIFFCQ IWHVGRVSNK DFQPNGEDPI SCTDRGLTPQ IRSNGIDIAH
    160 170 180 190 200
    FTRPRRLTTD EIPQIVNEFR VAARNAIEAG FDGVEIHGAH GYLIDQFMKD
    210 220 230 240 250
    QVNDRSDKYG GSLENRCRFA LEIVEAVANE IGSDRVGIRI SPFAHYNEAG
    260 270 280 290 300
    DTNPTALGLY MVESLNKYDL AYCHVVEPRM KTAWEKIECT ESLVPMRKAY
    310 320 330 340 350
    KGTFIVAGGY DREDGNRALI EDRADLVAYG RLFISNPDLP KRFELNAPLN
    360 370
    KYNRDTFYTS DPIVGYTDYP FLETMT
    Length:376
    Mass (Da):42,415
    Last modified:November 1, 1999 - v1
    Checksum:i83CFBEAC7CBC7A8F
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ242551 mRNA. Translation: CAB43506.1.
    RefSeqiNP_001234781.1. NM_001247852.1.
    UniGeneiLes.22.

    Genome annotation databases

    EnsemblPlantsiSolyc10g086220.1.1; Solyc10g086220.1.1; Solyc10g086220.1.
    GeneIDi544239.
    GrameneiSolyc10g086220.1.1; Solyc10g086220.1.1; Solyc10g086220.1.
    KEGGisly:544239.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ242551 mRNA. Translation: CAB43506.1.
    RefSeqiNP_001234781.1. NM_001247852.1.
    UniGeneiLes.22.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ICPX-ray1.90A/B1-376[»]
    1ICQX-ray2.00A/B1-376[»]
    1ICSX-ray2.30A/B1-376[»]
    3HGRX-ray2.30A/B1-376[»]
    ProteinModelPortaliQ9XG54.
    SMRiQ9XG54. Positions 10-373.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi4081.Solyc10g086220.1.1.

    Proteomic databases

    PaxDbiQ9XG54.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiSolyc10g086220.1.1; Solyc10g086220.1.1; Solyc10g086220.1.
    GeneIDi544239.
    GrameneiSolyc10g086220.1.1; Solyc10g086220.1.1; Solyc10g086220.1.
    KEGGisly:544239.

    Phylogenomic databases

    eggNOGiKOG0134. Eukaryota.
    COG1902. LUCA.
    InParanoidiQ9XG54.
    KOiK05894.
    OMAiECTESLV.

    Enzyme and pathway databases

    UniPathwayiUPA00382.
    BRENDAi1.3.1.42. 3101.

    Miscellaneous databases

    EvolutionaryTraceiQ9XG54.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR001155. OxRdtase_FMN_N.
    [Graphical view]
    PfamiPF00724. Oxidored_FMN. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. "A homolog of old yellow enzyme in tomato: spectral properties and substrate specificity of the recombinant protein."
      Strassner J., Fuerholz A., Macheroux P., Amrhein N., Schaller A.
      J. Biol. Chem. 274:35067-35073(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, CATALYTIC ACTIVITY.
      Strain: cv. Castlemart II.
      Tissue: Shoot.
    2. "Characterization and cDNA-microarray expression analysis of 12-oxophytodienoate reductases reveals differential roles for octadecanoid biosynthesis in the local versus the systemic wound response."
      Strassner J., Schaller F., Frick U.B., Howe G.A., Weiler E.W., Amrhein N., Macheroux P., Schaller A.
      Plant J. 32:585-601(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, COFACTOR, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION.
      Strain: cv. Castlemart II.
      Tissue: Shoot.
    3. "X-ray structure of 12-oxophytodienoate reductase 1 provides structural insight into substrate binding and specificity within the family of OYE."
      Breithaupt C., Strassner J., Breitinger U., Huber R., Macheroux P., Schaller A., Clausen T.
      Structure 9:419-429(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, SUBSTRATE SPECIFICITY, COFACTOR-BINDING.
    4. "Structural basis of substrate specificity of plant 12-oxophytodienoate reductases."
      Breithaupt C., Kurzbauer R., Schaller F., Stintzi A., Schaller A., Huber R., Macheroux P., Clausen T.
      J. Mol. Biol. 392:1266-1277(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH FMN.

    Entry informationi

    Entry nameiOPR1_SOLLC
    AccessioniPrimary (citable) accession number: Q9XG54
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2005
    Last sequence update: November 1, 1999
    Last modified: February 17, 2016
    This is version 77 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.