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Q9FEW9

- OPR3_SOLLC

UniProt

Q9FEW9 - OPR3_SOLLC

Protein

12-oxophytodienoate reductase 3

Gene

OPR3

Organism
Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 64 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Specifically cleaves olefinic bonds in cyclic enones. Involved in the biosynthesis of jasmonic acid (JA) and perhaps in biosynthesis or metabolism of other oxylipin signaling moleclules. It is required for the spatial and temporal regulation of JA levels during dehiscence of anthers, promoting the stomium degeneration program By similarity. In vitro, reduces 9S,13S-12-oxophytodienoic acid (9S,13S-OPDA) and 9R,13R-OPDA to 9S,13S-OPC-8:0 and 9R,13R-OPC-8:0, respectively.By similarity

    Catalytic activityi

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

    Cofactori

    FMN.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei64 – 641FMN; via amide nitrogen2 Publications
    Binding sitei106 – 1061FMN2 Publications
    Active sitei190 – 1901Proton donorBy similarity
    Binding sitei237 – 2371FMN2 Publications
    Binding sitei283 – 2831Substrate; via amide nitrogenBy similarity
    Binding sitei321 – 3211FMN; via amide nitrogen2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi31 – 333FMN2 Publications
    Nucleotide bindingi342 – 3432FMNBy similarity

    GO - Molecular functioni

    1. 12-oxophytodienoate reductase activity Source: UniProtKB-EC
    2. FMN binding Source: InterPro

    GO - Biological processi

    1. jasmonic acid biosynthetic process Source: EnsemblPlants/Gramene
    2. oxylipin biosynthetic process Source: UniProtKB-UniPathway
    3. response to fungus Source: EnsemblPlants/Gramene
    4. response to ozone Source: EnsemblPlants/Gramene

    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

    UniPathwayiUPA00382.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    12-oxophytodienoate reductase 3 (EC:1.3.1.42)
    Alternative name(s):
    12-oxophytodienoate-10,11-reductase 3
    Short name:
    OPDA-reductase 3
    LeOPR3
    Gene namesi
    Name:OPR3
    OrganismiSolanum lycopersicum (Tomato) (Lycopersicon esculentum)
    Taxonomic identifieri4081 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanumLycopersicon
    ProteomesiUP000004994: Chromosome 7

    Subcellular locationi

    Peroxisome 1 Publication

    GO - Cellular componenti

    1. peroxisome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 39639612-oxophytodienoate reductase 3PRO_0000194489Add
    BLAST

    Expressioni

    Tissue specificityi

    Expressed in roots and to lower extend in leaves and flowers.

    Inductioni

    By wounding, locally and systemically.

    Structurei

    Secondary structure

    1
    396
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi11 – 133
    Beta strandi16 – 183
    Beta strandi21 – 244
    Beta strandi26 – 294
    Helixi38 – 403
    Helixi44 – 5310
    Beta strandi59 – 613
    Beta strandi65 – 684
    Beta strandi74 – 763
    Helixi83 – 9816
    Beta strandi102 – 1087
    Helixi116 – 1183
    Helixi120 – 1223
    Beta strandi126 – 1283
    Beta strandi138 – 1403
    Beta strandi146 – 1483
    Helixi157 – 1593
    Helixi160 – 17617
    Beta strandi180 – 1856
    Helixi191 – 1966
    Turni198 – 2003
    Beta strandi208 – 2103
    Helixi211 – 22919
    Helixi231 – 2333
    Beta strandi234 – 2385
    Helixi244 – 2463
    Helixi252 – 27019
    Beta strandi275 – 2806
    Turni286 – 2894
    Beta strandi290 – 2923
    Turni293 – 2964
    Helixi297 – 31115
    Beta strandi312 – 3143
    Beta strandi316 – 3216
    Helixi324 – 3329
    Beta strandi337 – 3426
    Helixi343 – 3475
    Helixi351 – 3577
    Helixi366 – 3683
    Turni376 – 3783

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HS6X-ray1.90A/B1-396[»]
    2HS8X-ray1.90A/B1-396[»]
    2HSAX-ray1.50A/B1-396[»]
    3HGOX-ray2.30A/B1-396[»]
    3HGSX-ray2.00A/B1-396[»]
    ProteinModelPortaliQ9FEW9.
    SMRiQ9FEW9. Positions 10-385.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9FEW9.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni185 – 1884Substrate-bindingBy similarity
    Regioni342 – 3432FMN

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi394 – 3963Microbody targeting signalSequence Analysis

    Sequence similaritiesi

    Phylogenomic databases

    KOiK05894.
    OMAiRISHPEI.

    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.

    Q9FEW9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASSAQDGNN PLFSPYKMGK FNLSHRVVLA PMTRCRALNN IPQAALGEYY    50
    EQRATAGGFL ITEGTMISPT SAGFPHVPGI FTKEQVREWK KIVDVVHAKG 100
    AVIFCQLWHV GRASHEVYQP AGAAPISSTE KPISNRWRIL MPDGTHGIYP 150
    KPRAIGTYEI SQVVEDYRRS ALNAIEAGFD GIEIHGAHGY LIDQFLKDGI 200
    NDRTDEYGGS LANRCKFITQ VVQAVVSAIG ADRVGVRVSP AIDHLDAMDS 250
    NPLSLGLAVV ERLNKIQLHS GSKLAYLHVT QPRYVAYGQT EAGRLGSEEE 300
    EARLMRTLRN AYQGTFICSG GYTRELGIEA VAQGDADLVS YGRLFISNPD 350
    LVMRIKLNAP LNKYNRKTFY TQDPVVGYTD YPFLQGNGSN GPLSRL 396
    Length:396
    Mass (Da):43,520
    Last modified:March 1, 2001 - v1
    Checksum:iC9550E54D2EAF75B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ278332 mRNA. Translation: CAC21424.1.
    RefSeqiNP_001233873.1. NM_001246944.1.
    UniGeneiLes.3762.

    Genome annotation databases

    EnsemblPlantsiSolyc07g007870.2.1; Solyc07g007870.2.1; Solyc07g007870.2.
    GeneIDi543763.
    KEGGisly:543763.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ278332 mRNA. Translation: CAC21424.1 .
    RefSeqi NP_001233873.1. NM_001246944.1.
    UniGenei Les.3762.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2HS6 X-ray 1.90 A/B 1-396 [» ]
    2HS8 X-ray 1.90 A/B 1-396 [» ]
    2HSA X-ray 1.50 A/B 1-396 [» ]
    3HGO X-ray 2.30 A/B 1-396 [» ]
    3HGS X-ray 2.00 A/B 1-396 [» ]
    ProteinModelPortali Q9FEW9.
    SMRi Q9FEW9. Positions 10-385.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi Solyc07g007870.2.1 ; Solyc07g007870.2.1 ; Solyc07g007870.2 .
    GeneIDi 543763.
    KEGGi sly:543763.

    Phylogenomic databases

    KOi K05894.
    OMAi RISHPEI.

    Enzyme and pathway databases

    UniPathwayi UPA00382 .

    Miscellaneous databases

    EvolutionaryTracei Q9FEW9.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    InterProi IPR013785. Aldolase_TIM.
    IPR001155. OxRdtase_FMN_N.
    [Graphical view ]
    Pfami PF00724. Oxidored_FMN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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: NUCLEOTIDE SEQUENCE [MRNA], COFACTOR, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION.
      Strain: cv. Castlemart II.
      Tissue: Shoot.
    2. "Crystal structure of 12-oxophytodienoate reductase 3 from tomato: self-inhibition by dimerization."
      Breithaupt C., Kurzbauer R., Lilie H., Schaller A., Strassner J., Huber R., Macheroux P., Clausen T.
      Proc. Natl. Acad. Sci. U.S.A. 103:14337-14342(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH FMN.
    3. "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 (2.00 ANGSTROMS) IN COMPLEX WITH FMN.

    Entry informationi

    Entry nameiOPR3_SOLLC
    AccessioniPrimary (citable) accession number: Q9FEW9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2005
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 64 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

    External Data

    Dasty 3