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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.

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.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei64 – 641FMN; via amide nitrogen
Binding sitei106 – 1061FMN
Active sitei190 – 1901Proton donor By similarity
Binding sitei237 – 2371FMN
Binding sitei283 – 2831Substrate; via amide nitrogen By similarity
Binding sitei321 – 3211FMN; via amide nitrogen

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi31 – 333FMN
Nucleotide bindingi342 – 3432FMN By 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
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-SubCell
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 – 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.

Miscellaneous databases

EvolutionaryTraceiQ9FEW9.

Family & Domainsi

Region

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi394 – 3963Microbody targeting signal Reviewed prediction

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: May 14, 2014
This is version 63 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

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