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Protein

Peroxiredoxin-2E, chloroplastic

Gene

PRXIIE

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Reduces hydrogen peroxide and alkyl hydroperoxides with reducing equivalents provided through the thioredoxin or glutaredoxin system. May be involved in chloroplast redox homeostasis.

Catalytic activityi

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei121Cysteine sulfenic acid (-SOH) intermediateSequence analysis1

GO - Molecular functioni

GO - Biological processi

  • cell redox homeostasis Source: InterPro
  • defense response to bacterium Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

BioCyciARA:AT3G52960-MONOMER.

Protein family/group databases

PeroxiBasei4353. AtPrxII05.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin-2E, chloroplastic (EC:1.11.1.15)
Alternative name(s):
Peroxiredoxin IIE
Thioredoxin reductase 2E
Gene namesi
Name:PRXIIE
Ordered Locus Names:At3g52960
ORF Names:F8J2_130
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G52960.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast envelope Source: TAIR
  • chloroplast stroma Source: TAIR
  • plant-type cell wall Source: TAIR
  • plastid Source: TAIR
  • thylakoid Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 70ChloroplastSequence analysisAdd BLAST70
ChainiPRO_000028228171 – 234Peroxiredoxin-2E, chloroplasticAdd BLAST164

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei82PhosphoserineCombined sources1
Disulfide bondi121 ↔ 146Redox-active

Post-translational modificationi

The Cys-121-SH group is the primary site of oxidation by H2O2, and the oxidized Cys-121 (probably Cys-SOH) rapidly reacts with Cys-146-SH to form an intramolecular disulfide. This disulfide is subsequently reduced by thioredoxin to restore the reduced active form of the enzyme.

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiQ949U7.
PRIDEiQ949U7.

PTM databases

iPTMnetiQ949U7.
SwissPalmiQ949U7.

Expressioni

Tissue specificityi

Expressed in all tissues but predominantly in buds, siliques and seeds.2 Publications

Inductioni

Down-regulated by salt stress.1 Publication

Gene expression databases

GenevisibleiQ949U7. AT.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi9779. 3 interactors.
IntActiQ949U7. 1 interactor.
STRINGi3702.AT3G52960.1.

Structurei

3D structure databases

ProteinModelPortaliQ949U7.
SMRiQ949U7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini73 – 234ThioredoxinPROSITE-ProRule annotationAdd BLAST162

Sequence similaritiesi

Belongs to the peroxiredoxin 2 family.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

eggNOGiKOG0541. Eukaryota.
COG0678. LUCA.
HOGENOMiHOG000255884.
InParanoidiQ949U7.
OMAiYTTPRIS.
OrthoDBiEOG09360OQV.
PhylomeDBiQ949U7.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR013740. Redoxin.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF08534. Redoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q949U7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATSLSVSRF MSSSATVISV AKPLLSPTVS FTAPLSFTRS LAPNLSLKFR
60 70 80 90 100
NRRTNSASAT TRSFATTPVT ASISVGDKLP DSTLSYLDPS TGDVKTVTVS
110 120 130 140 150
SLTAGKKTIL FAVPGAFTPT CSQKHVPGFV SKAGELRSKG IDVIACISVN
160 170 180 190 200
DAFVMEAWRK DLGINDEVML LSDGNGEFTG KLGVELDLRD KPVGLGVRSR
210 220 230
RYAILADDGV VKVLNLEEGG AFTNSSAEDM LKAL
Length:234
Mass (Da):24,684
Last modified:April 3, 2007 - v2
Checksum:i4F66DA63CD15F003
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti133A → V in AAK92817 (PubMed:14593172).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL132969 Genomic DNA. Translation: CAB86900.1.
CP002686 Genomic DNA. Translation: AEE79018.1.
AY050880 mRNA. Translation: AAK92817.1.
AY054638 mRNA. Translation: AAK96829.1.
AY072493 mRNA. Translation: AAL66908.1.
AY150397 mRNA. Translation: AAN12942.1.
PIRiPA0047.
T47553.
RefSeqiNP_190864.1. NM_115156.3.
UniGeneiAt.9858.

Genome annotation databases

EnsemblPlantsiAT3G52960.1; AT3G52960.1; AT3G52960.
GeneIDi824462.
GrameneiAT3G52960.1; AT3G52960.1; AT3G52960.
KEGGiath:AT3G52960.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL132969 Genomic DNA. Translation: CAB86900.1.
CP002686 Genomic DNA. Translation: AEE79018.1.
AY050880 mRNA. Translation: AAK92817.1.
AY054638 mRNA. Translation: AAK96829.1.
AY072493 mRNA. Translation: AAL66908.1.
AY150397 mRNA. Translation: AAN12942.1.
PIRiPA0047.
T47553.
RefSeqiNP_190864.1. NM_115156.3.
UniGeneiAt.9858.

3D structure databases

ProteinModelPortaliQ949U7.
SMRiQ949U7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi9779. 3 interactors.
IntActiQ949U7. 1 interactor.
STRINGi3702.AT3G52960.1.

Protein family/group databases

PeroxiBasei4353. AtPrxII05.

PTM databases

iPTMnetiQ949U7.
SwissPalmiQ949U7.

Proteomic databases

PaxDbiQ949U7.
PRIDEiQ949U7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G52960.1; AT3G52960.1; AT3G52960.
GeneIDi824462.
GrameneiAT3G52960.1; AT3G52960.1; AT3G52960.
KEGGiath:AT3G52960.

Organism-specific databases

TAIRiAT3G52960.

Phylogenomic databases

eggNOGiKOG0541. Eukaryota.
COG0678. LUCA.
HOGENOMiHOG000255884.
InParanoidiQ949U7.
OMAiYTTPRIS.
OrthoDBiEOG09360OQV.
PhylomeDBiQ949U7.

Enzyme and pathway databases

BioCyciARA:AT3G52960-MONOMER.

Miscellaneous databases

PROiQ949U7.

Gene expression databases

GenevisibleiQ949U7. AT.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR013740. Redoxin.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF08534. Redoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPRX2E_ARATH
AccessioniPrimary (citable) accession number: Q949U7
Secondary accession number(s): Q9LF96
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: April 3, 2007
Last modified: November 30, 2016
This is version 105 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

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. 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.