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Protein

12-oxophytodienoate reductase 3

Gene

OPR3

Organism
Arabidopsis thaliana (Mouse-ear cress)
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. Required for the spatial and temporal regulation of JA levels during dehiscence of anthers, promoting the stomium degeneration program. 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. Can detoxify the explosive 2,4,6-trinitrotoluene (TNT) in vitro by catalyzing its nitroreduction to form hydroxylamino-dinitrotoluene (HADNT).2 Publications

Catalytic activityi

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

Cofactori

Kineticsi

  1. KM=35 µM for (9S,13S)-OPDA2 Publications
  2. KM=2.5 mM for cyclohexenone2 Publications
  3. KM=12 µM for NADPH2 Publications
  1. Vmax=53.7 nmol/sec/mg enzyme with (9S,13S)-OPDA as substrate2 Publications

pH dependencei

Optimum pH is 7-8. Active from pH 5.0 to 8.5.2 Publications

Pathwayi: oxylipin 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)DescriptionActionsGraphical viewLength
Binding sitei64FMN; via amide nitrogen3 Publications1
Binding sitei106FMN3 Publications1
Active sitei191Proton donorBy similarity1
Binding sitei238FMN3 Publications1
Binding sitei284Substrate; via amide nitrogen1 Publication1
Binding sitei322FMN; via amide nitrogen3 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi31 – 33FMN3 Publications3
Nucleotide bindingi343 – 344FMN3 Publications2

GO - Molecular functioni

GO - Biological processi

  • fatty acid biosynthetic process Source: UniProtKB-KW
  • jasmonic acid biosynthetic process Source: TAIR
  • oxylipin biosynthetic process Source: GO_Central
  • response to fungus Source: TAIR
  • response to ozone Source: TAIR
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

BioCyciARA:GQT-1160-MONOMER.
MetaCyc:AT2G06050-MONOMER.
BRENDAi1.3.1.42. 399.
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:
AtOPR3
Short name:
OPDA-reductase 3
Delayed dehiscence 1
Cleaved into the following chain:
Gene namesi
Name:OPR3
Synonyms:DDE1
Ordered Locus Names:At2g06050
ORF Names:F5K7.19
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G06050.

Subcellular locationi

GO - Cellular componenti

  • peroxisome Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Disruption phenotypei

Male sterility. Fertility can be restored by exogenous jasmonate but not by 12-oxophytodienoic acid. Large petals with altered vein patterning.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004343611 – 39112-oxophytodienoate reductase 3Add BLAST391
Initiator methionineiRemoved; alternateCombined sources
ChainiPRO_00001944852 – 39112-oxophytodienoate reductase 3, N-terminally processedAdd BLAST390

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei2N-acetylthreonine; in 12-oxophytodienoate reductase 3, N-terminally processedCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ9FUP0.
PRIDEiQ9FUP0.

Expressioni

Tissue specificityi

Expressed in green seedling, leaves, flowers (anthers, pistil, petal and stamen), and to a lower extent in roots and siliques. Specifically expressed in filament during anther dehiscence initiation.3 Publications

Developmental stagei

At the initiation time of the stomium degeneration program, expressed in all floral organs. Later, transcripts levels increase in pistil, petal, stamen filament, and in vascular region close to the stamen filament. When the anther dehiscence is initiated, levels of transcripts decrease, except within the vascular tissues.1 Publication

Inductioni

Induction mediated by wounding and methyl JA (MeJA) needs COI1. Also induced by BR (24-epibrassinolide), UV LIGHT, wind, touch, and the detergent Sapogenat T-110. Seems to not be influenced by salicylic acid, cold and heat treatments.2 Publications

Gene expression databases

GenevisibleiQ9FUP0. AT.

Interactioni

Protein-protein interaction databases

BioGridi559. 2 interactors.
IntActiQ9FUP0. 3 interactors.
STRINGi3702.AT2G06050.1.

Structurei

Secondary structure

1391
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi16 – 18Combined sources3
Beta strandi21 – 24Combined sources4
Beta strandi26 – 29Combined sources4
Helixi38 – 40Combined sources3
Helixi44 – 52Combined sources9
Beta strandi59 – 68Combined sources10
Helixi83 – 98Combined sources16
Beta strandi102 – 108Combined sources7
Helixi116 – 118Combined sources3
Helixi120 – 122Combined sources3
Beta strandi126 – 130Combined sources5
Turni135 – 137Combined sources3
Helixi158 – 160Combined sources3
Helixi161 – 178Combined sources18
Beta strandi181 – 187Combined sources7
Helixi192 – 197Combined sources6
Turni199 – 201Combined sources3
Beta strandi209 – 211Combined sources3
Helixi212 – 230Combined sources19
Helixi232 – 234Combined sources3
Beta strandi235 – 239Combined sources5
Helixi245 – 247Combined sources3
Helixi253 – 269Combined sources17
Beta strandi276 – 281Combined sources6
Helixi301 – 312Combined sources12
Beta strandi313 – 315Combined sources3
Beta strandi317 – 322Combined sources6
Helixi325 – 333Combined sources9
Beta strandi338 – 343Combined sources6
Helixi344 – 348Combined sources5
Helixi352 – 357Combined sources6
Helixi367 – 369Combined sources3
Turni377 – 379Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Q45X-ray2.00A/B1-391[»]
2G5WX-ray2.58A/B1-391[»]
2Q3OX-ray2.00A/B1-391[»]
ProteinModelPortaliQ9FUP0.
SMRiQ9FUP0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9FUP0.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni186 – 189Substrate-binding4

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi389 – 391Microbody targeting signalSequence analysis3

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0134. Eukaryota.
COG1902. LUCA.
HOGENOMiHOG000116231.
InParanoidiQ9FUP0.
KOiK05894.
OMAiRIVKMEC.
OrthoDBiEOG09360FPQ.
PhylomeDBiQ9FUP0.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9FUP0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAAQGNSNE TLFSSYKMGR FDLSHRVVLA PMTRCRALNG VPNAALAEYY
60 70 80 90 100
AQRTTPGGFL ISEGTMVSPG SAGFPHVPGI YSDEQVEAWK QVVEAVHAKG
110 120 130 140 150
GFIFCQLWHV GRASHAVYQP NGGSPISSTN KPISENRWRV LLPDGSHVKY
160 170 180 190 200
PKPRALEASE IPRVVEDYCL SALNAIRAGF DGIEIHGAHG YLIDQFLKDG
210 220 230 240 250
INDRTDQYGG SIANRCRFLK QVVEGVVSAI GASKVGVRVS PAIDHLDATD
260 270 280 290 300
SDPLSLGLAV VGMLNKLQGV NGSKLAYLHV TQPRYHAYGQ TESGRQGSDE
310 320 330 340 350
EEAKLMKSLR MAYNGTFMSS GGFNKELGMQ AVQQGDADLV SYGRLFIANP
360 370 380 390
DLVSRFKIDG ELNKYNRKTF YTQDPVVGYT DYPFLAPFSR L
Length:391
Mass (Da):42,691
Last modified:April 26, 2005 - v2
Checksum:i5E1D9888324101D7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti213A → E in AAD38925 (PubMed:11094980).Curated1
Sequence conflicti213A → E in AAF67635 (PubMed:10899973).Curated1
Sequence conflicti213A → E in AAG15379 (PubMed:10973494).Curated1
Sequence conflicti252D → N in AAD38925 (PubMed:11094980).Curated1
Sequence conflicti252D → N in AAF67635 (PubMed:10899973).Curated1
Sequence conflicti252D → N in AAG15379 (PubMed:10973494).Curated1
Sequence conflicti252D → N in CAB66143 (Ref. 4) Curated1
Sequence conflicti262G → D in AAD38925 (PubMed:11094980).Curated1
Sequence conflicti262G → D in AAF67635 (PubMed:10899973).Curated1
Sequence conflicti262G → D in AAG15379 (PubMed:10973494).Curated1
Sequence conflicti262G → D in CAB66143 (Ref. 4) Curated1
Sequence conflicti269G → D in AAD38925 (PubMed:11094980).Curated1
Sequence conflicti269G → D in AAF67635 (PubMed:10899973).Curated1
Sequence conflicti269G → D in AAG15379 (PubMed:10973494).Curated1
Sequence conflicti269G → D in CAB66143 (Ref. 4) Curated1
Sequence conflicti273S → L in AAD38925 (PubMed:11094980).Curated1
Sequence conflicti273S → L in AAF67635 (PubMed:10899973).Curated1
Sequence conflicti273S → L in AAG15379 (PubMed:10973494).Curated1
Sequence conflicti273S → L in CAB66143 (Ref. 4) Curated1
Sequence conflicti314N → K in AAD38925 (PubMed:11094980).Curated1
Sequence conflicti314N → K in AAF67635 (PubMed:10899973).Curated1
Sequence conflicti314N → K in AAG15379 (PubMed:10973494).Curated1
Sequence conflicti314N → K in CAB66143 (Ref. 4) Curated1
Sequence conflicti361E → K in AAF67635 (PubMed:10899973).Curated1
Sequence conflicti361E → K in AAG15379 (PubMed:10973494).Curated1
Sequence conflicti388F → S in AAD38925 (PubMed:11094980).Curated1
Sequence conflicti388F → S in AAG15379 (PubMed:10973494).Curated1
Sequence conflicti388F → S in CAB66143 (Ref. 4) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF132212 mRNA. Translation: AAD38925.1.
AF218257 Genomic DNA. Translation: AAF67635.1.
AF293653 mRNA. Translation: AAG15379.1.
AJ238149 mRNA. Translation: CAB66143.1.
AC006413 Genomic DNA. Translation: AAD19764.1.
CP002685 Genomic DNA. Translation: AEC05998.1.
CP002685 Genomic DNA. Translation: AEC05999.1.
CP002685 Genomic DNA. Translation: AEC06000.1.
AF370582 mRNA. Translation: AAK43901.1.
AF410322 mRNA. Translation: AAK95308.1.
AY097367 mRNA. Translation: AAM19883.1.
AK317250 mRNA. Translation: BAH19929.1.
PIRiF84474.
RefSeqiNP_001077884.1. NM_001084415.2.
NP_178662.1. NM_126619.4.
NP_973431.1. NM_201702.2.
UniGeneiAt.1135.
At.24306.
At.74949.

Genome annotation databases

EnsemblPlantsiAT2G06050.1; AT2G06050.1; AT2G06050.
AT2G06050.2; AT2G06050.2; AT2G06050.
AT2G06050.3; AT2G06050.3; AT2G06050.
GeneIDi815160.
GrameneiAT2G06050.1; AT2G06050.1; AT2G06050.
AT2G06050.2; AT2G06050.2; AT2G06050.
AT2G06050.3; AT2G06050.3; AT2G06050.
KEGGiath:AT2G06050.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF132212 mRNA. Translation: AAD38925.1.
AF218257 Genomic DNA. Translation: AAF67635.1.
AF293653 mRNA. Translation: AAG15379.1.
AJ238149 mRNA. Translation: CAB66143.1.
AC006413 Genomic DNA. Translation: AAD19764.1.
CP002685 Genomic DNA. Translation: AEC05998.1.
CP002685 Genomic DNA. Translation: AEC05999.1.
CP002685 Genomic DNA. Translation: AEC06000.1.
AF370582 mRNA. Translation: AAK43901.1.
AF410322 mRNA. Translation: AAK95308.1.
AY097367 mRNA. Translation: AAM19883.1.
AK317250 mRNA. Translation: BAH19929.1.
PIRiF84474.
RefSeqiNP_001077884.1. NM_001084415.2.
NP_178662.1. NM_126619.4.
NP_973431.1. NM_201702.2.
UniGeneiAt.1135.
At.24306.
At.74949.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Q45X-ray2.00A/B1-391[»]
2G5WX-ray2.58A/B1-391[»]
2Q3OX-ray2.00A/B1-391[»]
ProteinModelPortaliQ9FUP0.
SMRiQ9FUP0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi559. 2 interactors.
IntActiQ9FUP0. 3 interactors.
STRINGi3702.AT2G06050.1.

Proteomic databases

PaxDbiQ9FUP0.
PRIDEiQ9FUP0.

Protocols and materials databases

DNASUi815160.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G06050.1; AT2G06050.1; AT2G06050.
AT2G06050.2; AT2G06050.2; AT2G06050.
AT2G06050.3; AT2G06050.3; AT2G06050.
GeneIDi815160.
GrameneiAT2G06050.1; AT2G06050.1; AT2G06050.
AT2G06050.2; AT2G06050.2; AT2G06050.
AT2G06050.3; AT2G06050.3; AT2G06050.
KEGGiath:AT2G06050.

Organism-specific databases

TAIRiAT2G06050.

Phylogenomic databases

eggNOGiKOG0134. Eukaryota.
COG1902. LUCA.
HOGENOMiHOG000116231.
InParanoidiQ9FUP0.
KOiK05894.
OMAiRIVKMEC.
OrthoDBiEOG09360FPQ.
PhylomeDBiQ9FUP0.

Enzyme and pathway databases

UniPathwayiUPA00382.
BioCyciARA:GQT-1160-MONOMER.
MetaCyc:AT2G06050-MONOMER.
BRENDAi1.3.1.42. 399.

Miscellaneous databases

EvolutionaryTraceiQ9FUP0.
PROiQ9FUP0.

Gene expression databases

GenevisibleiQ9FUP0. AT.

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...

Entry informationi

Entry nameiOPR3_ARATH
AccessioniPrimary (citable) accession number: Q9FUP0
Secondary accession number(s): B9DGR2
, Q9LLD6, Q9SCY4, Q9XHD2, Q9ZQ01
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: April 26, 2005
Last modified: November 30, 2016
This is version 118 of the entry and version 2 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. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.