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Q9FEW9

- OPR3_SOLLC

UniProt

Q9FEW9 - OPR3_SOLLC

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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

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

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: EnsemblPlants/Gramene

GO - Biological processi

  1. abscisic acid-activated signaling pathway Source: EnsemblPlants/Gramene
  2. hyperosmotic salinity response Source: EnsemblPlants/Gramene
  3. indoleacetic acid biosynthetic process Source: EnsemblPlants/Gramene
  4. jasmonic acid biosynthetic process Source: EnsemblPlants/Gramene
  5. jasmonic acid mediated signaling pathway Source: EnsemblPlants/Gramene
  6. oxylipin biosynthetic process Source: UniProtKB-UniPathway
  7. response to auxin Source: EnsemblPlants/Gramene
  8. response to ethylene Source: EnsemblPlants/Gramene
  9. response to water deprivation Source: EnsemblPlants/Gramene
  10. response to wounding Source: EnsemblPlants/Gramene
  11. tryptophan catabolic process Source: EnsemblPlants/Gramene
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

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-KW
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.

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.
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

        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 .
RefSeqi NP_001233873.1. NM_001246944.1.
UniGenei Les.3762.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

InParanoidi Q9FEW9.
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: November 26, 2014
This is version 66 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