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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei64 – 641FMN; via amide nitrogen3 Publications
Binding sitei106 – 1061FMN3 Publications
Active sitei191 – 1911Proton donorBy similarity
Binding sitei238 – 2381FMN3 Publications
Binding sitei284 – 2841Substrate; via amide nitrogen1 Publication
Binding sitei322 – 3221FMN; via amide nitrogen3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi31 – 333FMN3 Publications
Nucleotide bindingi343 – 3442FMN3 Publications

GO - Molecular functioni

GO - Biological processi

  • 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-1159-MONOMER.
ARA: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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 39139112-oxophytodienoate reductase 3PRO_0000434361Add
BLAST
Initiator methionineiRemoved; alternateCombined sources
Chaini2 – 39139012-oxophytodienoate reductase 3, N-terminally processedPRO_0000194485Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei2 – 21N-acetylthreonine; in 12-oxophytodienoate reductase 3, N-terminally processedCombined sources

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 interactions.
IntActiQ9FUP0. 3 interactions.
STRINGi3702.AT2G06050.1.

Structurei

Secondary structure

1
391
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi16 – 183Combined sources
Beta strandi21 – 244Combined sources
Beta strandi26 – 294Combined sources
Helixi38 – 403Combined sources
Helixi44 – 529Combined sources
Beta strandi59 – 6810Combined sources
Helixi83 – 9816Combined sources
Beta strandi102 – 1087Combined sources
Helixi116 – 1183Combined sources
Helixi120 – 1223Combined sources
Beta strandi126 – 1305Combined sources
Turni135 – 1373Combined sources
Helixi158 – 1603Combined sources
Helixi161 – 17818Combined sources
Beta strandi181 – 1877Combined sources
Helixi192 – 1976Combined sources
Turni199 – 2013Combined sources
Beta strandi209 – 2113Combined sources
Helixi212 – 23019Combined sources
Helixi232 – 2343Combined sources
Beta strandi235 – 2395Combined sources
Helixi245 – 2473Combined sources
Helixi253 – 26917Combined sources
Beta strandi276 – 2816Combined sources
Helixi301 – 31212Combined sources
Beta strandi313 – 3153Combined sources
Beta strandi317 – 3226Combined sources
Helixi325 – 3339Combined sources
Beta strandi338 – 3436Combined sources
Helixi344 – 3485Combined sources
Helixi352 – 3576Combined sources
Helixi367 – 3693Combined sources
Turni377 – 3793Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q45X-ray2.00A/B1-391[»]
2G5WX-ray2.58A/B1-391[»]
2Q3OX-ray2.00A/B1-391[»]
ProteinModelPortaliQ9FUP0.
SMRiQ9FUP0. Positions 9-385.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9FUP0.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni186 – 1894Substrate-binding

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi389 – 3913Microbody targeting signalSequence analysis

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti213 – 2131A → E in AAD38925 (PubMed:11094980).Curated
Sequence conflicti213 – 2131A → E in AAF67635 (PubMed:10899973).Curated
Sequence conflicti213 – 2131A → E in AAG15379 (PubMed:10973494).Curated
Sequence conflicti252 – 2521D → N in AAD38925 (PubMed:11094980).Curated
Sequence conflicti252 – 2521D → N in AAF67635 (PubMed:10899973).Curated
Sequence conflicti252 – 2521D → N in AAG15379 (PubMed:10973494).Curated
Sequence conflicti252 – 2521D → N in CAB66143 (Ref. 4) Curated
Sequence conflicti262 – 2621G → D in AAD38925 (PubMed:11094980).Curated
Sequence conflicti262 – 2621G → D in AAF67635 (PubMed:10899973).Curated
Sequence conflicti262 – 2621G → D in AAG15379 (PubMed:10973494).Curated
Sequence conflicti262 – 2621G → D in CAB66143 (Ref. 4) Curated
Sequence conflicti269 – 2691G → D in AAD38925 (PubMed:11094980).Curated
Sequence conflicti269 – 2691G → D in AAF67635 (PubMed:10899973).Curated
Sequence conflicti269 – 2691G → D in AAG15379 (PubMed:10973494).Curated
Sequence conflicti269 – 2691G → D in CAB66143 (Ref. 4) Curated
Sequence conflicti273 – 2731S → L in AAD38925 (PubMed:11094980).Curated
Sequence conflicti273 – 2731S → L in AAF67635 (PubMed:10899973).Curated
Sequence conflicti273 – 2731S → L in AAG15379 (PubMed:10973494).Curated
Sequence conflicti273 – 2731S → L in CAB66143 (Ref. 4) Curated
Sequence conflicti314 – 3141N → K in AAD38925 (PubMed:11094980).Curated
Sequence conflicti314 – 3141N → K in AAF67635 (PubMed:10899973).Curated
Sequence conflicti314 – 3141N → K in AAG15379 (PubMed:10973494).Curated
Sequence conflicti314 – 3141N → K in CAB66143 (Ref. 4) Curated
Sequence conflicti361 – 3611E → K in AAF67635 (PubMed:10899973).Curated
Sequence conflicti361 – 3611E → K in AAG15379 (PubMed:10973494).Curated
Sequence conflicti388 – 3881F → S in AAD38925 (PubMed:11094980).Curated
Sequence conflicti388 – 3881F → S in AAG15379 (PubMed:10973494).Curated
Sequence conflicti388 – 3881F → S in CAB66143 (Ref. 4) Curated

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_001084415.1.
NP_178662.1. NM_126619.3.
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_001084415.1.
NP_178662.1. NM_126619.3.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q45X-ray2.00A/B1-391[»]
2G5WX-ray2.58A/B1-391[»]
2Q3OX-ray2.00A/B1-391[»]
ProteinModelPortaliQ9FUP0.
SMRiQ9FUP0. Positions 9-385.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi559. 2 interactions.
IntActiQ9FUP0. 3 interactions.
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-1159-MONOMER.
ARA: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: September 7, 2016
This is version 115 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.