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Protein

12-oxophytodienoate reductase 3

Gene

OPR3

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 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

FMNBy similarity

Pathway:ioxylipin 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 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

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 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 Componenti: Chromosome 7

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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.

Interactioni

Protein-protein interaction databases

DIPiDIP-61271N.
STRINGi4081.Solyc07g007870.2.1.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

InParanoidiQ9FEW9.
KOiK05894.
OMAiAYFNMAT.

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

        10         20         30         40         50
MASSAQDGNN PLFSPYKMGK FNLSHRVVLA PMTRCRALNN IPQAALGEYY
60 70 80 90 100
EQRATAGGFL ITEGTMISPT SAGFPHVPGI FTKEQVREWK KIVDVVHAKG
110 120 130 140 150
AVIFCQLWHV GRASHEVYQP AGAAPISSTE KPISNRWRIL MPDGTHGIYP
160 170 180 190 200
KPRAIGTYEI SQVVEDYRRS ALNAIEAGFD GIEIHGAHGY LIDQFLKDGI
210 220 230 240 250
NDRTDEYGGS LANRCKFITQ VVQAVVSAIG ADRVGVRVSP AIDHLDAMDS
260 270 280 290 300
NPLSLGLAVV ERLNKIQLHS GSKLAYLHVT QPRYVAYGQT EAGRLGSEEE
310 320 330 340 350
EARLMRTLRN AYQGTFICSG GYTRELGIEA VAQGDADLVS YGRLFISNPD
360 370 380 390
LVMRIKLNAP LNKYNRKTFY TQDPVVGYTD YPFLQGNGSN GPLSRL
Length:396
Mass (Da):43,520
Last modified:March 1, 2001 - v1
Checksum:iC9550E54D2EAF75B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AJ278332 mRNA. Translation: CAC21424.1.
RefSeqiNP_001233873.1. NM_001246944.1.
UniGeneiLes.3762.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

DIPiDIP-61271N.
STRINGi4081.Solyc07g007870.2.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

InParanoidiQ9FEW9.
KOiK05894.
OMAiAYFNMAT.

Enzyme and pathway databases

UniPathwayiUPA00382.
BRENDAi1.3.1.42. 3101.

Miscellaneous databases

EvolutionaryTraceiQ9FEW9.

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. "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: July 22, 2015
This is version 72 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

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 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.