Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 138 (26 Feb 2020)
Sequence version 2 (26 Apr 2005)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

12-oxophytodienoate reductase 3

Gene

OPR3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Specifically cleaves olefinic bonds in cyclic enones (PubMed:11094980). Involved in the biosynthesis of jasmonic acid (JA) and perhaps in biosynthesis or metabolism of other oxylipin signaling moleclules (PubMed:29291349, PubMed:10872231, PubMed:10973494). Required for the spatial and temporal regulation of JA levels during dehiscence of anthers, promoting the stomium degeneration program (PubMed:10899973, PubMed:10973494). 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 (PubMed:10872231). Can detoxify the explosive 2,4,6-trinitrotoluene (TNT) in vitro by catalyzing its nitroreduction to form hydroxylamino-dinitrotoluene (HADNT) (PubMed:19605548).6 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

FMN2 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: oxylipin biosynthesis

This protein is involved in the pathway oxylipin biosynthesis, which is part of Lipid metabolism.Curated
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
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei64FMN; via amide nitrogenCombined sources2 Publications1
Binding sitei106FMNCombined sources3 Publications1
Binding sitei186SubstrateCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei191Proton donor1 Publication1
Binding sitei238FMNCombined sources3 Publications1
Binding sitei284Substrate; via amide nitrogenCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi31 – 33FMNCombined sources3 Publications3
Nucleotide bindingi320 – 322FMNCombined sources3 Publications3
Nucleotide bindingi343 – 344FMNCombined sources3 Publications2

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Oxylipin biosynthesis
LigandFlavoprotein, FMN, NADP

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
ARA:GQT-1160-MONOMER
MetaCyc:AT2G06050-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.3.1.42 399

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00382

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000001780

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
12-oxophytodienoate reductase 31 Publication (EC:1.3.1.423 Publications)
Alternative name(s):
12-oxophytodienoate-10,11-reductase 31 Publication
Short name:
AtOPR31 Publication
Short name:
OPDA-reductase 31 Publication
Protein DELAYED DEHISCENCE 11 Publication
Cleaved into the following chain:
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:OPR31 Publication
Synonyms:DDE11 Publication
Ordered Locus Names:At2g06050Imported
ORF Names:F5K7.19Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiArabidopsis thaliana (Mouse-ear cress)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri3702 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000007605 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2, ARATH_2
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

Arabidopsis Information Portal

More...
Araporti
AT2G06050

The Arabidopsis Information Resource

More...
TAIRi
locus:2051516 AT2G06050

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Peroxisome

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Male sterility (PubMed:10973494, PubMed:19765234, PubMed:29291349). Fertility can be restored by exogenous jasmonate but not by 12-oxophytodienoic acid (PubMed:10973494, PubMed:19765234, PubMed:29291349). Large petals with altered vein patterning (PubMed:19765234).3 Publications

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004343611 – 39112-oxophytodienoate reductase 3Add BLAST391
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved; alternateCombined sources
ChainiPRO_00001944852 – 39112-oxophytodienoate reductase 3, N-terminally processedAdd BLAST390

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1N-acetylmethionineBy similarity1
Modified residuei2N-acetylthreonine; in 12-oxophytodienoate reductase 3, N-terminally processedCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q9FUP0

PRoteomics IDEntifications database

More...
PRIDEi
Q9FUP0

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9FUP0

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>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

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>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 (PubMed:11094980, Ref. 4). Induced by infection with the fungal pathogens Botritys cinerea and Alternaria brassicicola, insect feeding with Spodoptera littoralis, and wounding (PubMed:29291349).3 Publications

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q9FUP0 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9FUP0 AT

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
559, 2 interactors

Protein interaction database and analysis system

More...
IntActi
Q9FUP0, 3 interactors

STRING: functional protein association networks

More...
STRINGi
3702.AT2G06050.2

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1391
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q9FUP0

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q9FUP0

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi389 – 391Microbody targeting signalSequence analysis3

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0134 Eukaryota
COG1902 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_012153_0_2_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9FUP0

KEGG Orthology (KO)

More...
KOi
K05894

Identification of Orthologs from Complete Genome Data

More...
OMAi
QPKGHVS

Database of Orthologous Groups

More...
OrthoDBi
978998at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9FUP0

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.20.20.70, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR013785 Aldolase_TIM
IPR001155 OxRdtase_FMN_N

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00724 Oxidored_FMN, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i5E1D9888324101D7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

Protein sequence database of the Protein Information Resource

More...
PIRi
F84474

NCBI Reference Sequences

More...
RefSeqi
NP_001077884.1, NM_001084415.2
NP_178662.1, NM_126619.4
NP_973431.1, NM_201702.2

Genome annotation databases

Ensembl plant genome annotation project

More...
EnsemblPlantsi
AT2G06050.1; AT2G06050.1; AT2G06050
AT2G06050.2; AT2G06050.2; AT2G06050
AT2G06050.3; AT2G06050.3; AT2G06050

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
815160

Gramene; a comparative resource for plants

More...
Gramenei
AT2G06050.1; AT2G06050.1; AT2G06050
AT2G06050.2; AT2G06050.2; AT2G06050
AT2G06050.3; AT2G06050.3; AT2G06050

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ath:AT2G06050

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Q45X-ray2.00A/B1-391[»]
2G5WX-ray2.58A/B1-391[»]
2Q3OX-ray2.00A/B1-391[»]
SMRiQ9FUP0
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

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

Chemistry databases

SwissLipidsiSLP:000001780

PTM databases

iPTMnetiQ9FUP0

Proteomic databases

PaxDbiQ9FUP0
PRIDEiQ9FUP0

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
815160

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

AraportiAT2G06050
TAIRilocus:2051516 AT2G06050

Phylogenomic databases

eggNOGiKOG0134 Eukaryota
COG1902 LUCA
HOGENOMiCLU_012153_0_2_1
InParanoidiQ9FUP0
KOiK05894
OMAiQPKGHVS
OrthoDBi978998at2759
PhylomeDBiQ9FUP0

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiQ9FUP0

Protein Ontology

More...
PROi
PR:Q9FUP0

Gene expression databases

ExpressionAtlasiQ9FUP0 baseline and differential
GenevisibleiQ9FUP0 AT

Family and domain databases

Gene3Di3.20.20.70, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR001155 OxRdtase_FMN_N
PfamiView protein in Pfam
PF00724 Oxidored_FMN, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiOPR3_ARATH
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9FUP0
Secondary accession number(s): B9DGR2
, Q9LLD6, Q9SCY4, Q9XHD2, Q9ZQ01
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: April 26, 2005
Last modified: February 26, 2020
This is version 138 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, 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
  4. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again