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Q9FEW9 (OPR3_SOLLC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:OPR3
OrganismSolanum lycopersicum (Tomato) (Lycopersicon esculentum) [Reference proteome]
Taxonomic identifier4081 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanumLycopersicon

Protein attributes

Sequence length396 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Cofactor

FMN By similarity. Ref.1

Pathway

Lipid metabolism; oxylipin biosynthesis.

Subcellular location

Peroxisome Ref.1.

Tissue specificity

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

Induction

By wounding, locally and systemically.

Sequence similarities

Belongs to the NADH:flavin oxidoreductase/NADH oxidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 39639612-oxophytodienoate reductase 3
PRO_0000194489

Regions

Nucleotide binding31 – 333FMN
Nucleotide binding342 – 3432FMN By similarity
Region185 – 1884Substrate-binding By similarity
Region342 – 3432FMN
Motif394 – 3963Microbody targeting signal Potential

Sites

Active site1901Proton donor By similarity
Binding site641FMN; via amide nitrogen
Binding site1061FMN
Binding site2371FMN
Binding site2831Substrate; via amide nitrogen By similarity
Binding site3211FMN; via amide nitrogen

Secondary structure

......................................................................... 396
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9FEW9 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: C9550E54D2EAF75B

FASTA39643,520
        10         20         30         40         50         60 
MASSAQDGNN PLFSPYKMGK FNLSHRVVLA PMTRCRALNN IPQAALGEYY EQRATAGGFL 

        70         80         90        100        110        120 
ITEGTMISPT SAGFPHVPGI FTKEQVREWK KIVDVVHAKG AVIFCQLWHV GRASHEVYQP 

       130        140        150        160        170        180 
AGAAPISSTE KPISNRWRIL MPDGTHGIYP KPRAIGTYEI SQVVEDYRRS ALNAIEAGFD 

       190        200        210        220        230        240 
GIEIHGAHGY LIDQFLKDGI NDRTDEYGGS LANRCKFITQ VVQAVVSAIG ADRVGVRVSP 

       250        260        270        280        290        300 
AIDHLDAMDS NPLSLGLAVV ERLNKIQLHS GSKLAYLHVT QPRYVAYGQT EAGRLGSEEE 

       310        320        330        340        350        360 
EARLMRTLRN AYQGTFICSG GYTRELGIEA VAQGDADLVS YGRLFISNPD LVMRIKLNAP 

       370        380        390 
LNKYNRKTFY TQDPVVGYTD YPFLQGNGSN GPLSRL 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ278332 mRNA. Translation: CAC21424.1.
RefSeqNP_001233873.1. NM_001246944.1.
UniGeneLes.3762.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ9FEW9.
SMRQ9FEW9. Positions 10-385.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsSolyc07g007870.2.1; Solyc07g007870.2.1; Solyc07g007870.2.
GeneID543763.
KEGGsly:543763.

Phylogenomic databases

KOK05894.
OMARISHPEI.

Enzyme and pathway databases

UniPathwayUPA00382.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR001155. OxRdtase_FMN_N.
[Graphical view]
PfamPF00724. Oxidored_FMN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9FEW9.

Entry information

Entry nameOPR3_SOLLC
AccessionPrimary (citable) accession number: Q9FEW9
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways