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Protein

Thioredoxin reductase 2

Gene

NTR2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Possesses thioredoxin-disulfide reductase activity towards thioredoxins O1, O2 and F3.1 Publication

Catalytic activityi

Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.

Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei109FADBy similarity1
Binding sitei142FAD; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei200FADBy similarity1
Binding sitei345FADBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi66 – 69FADBy similarity4
Nucleotide bindingi87 – 88FADBy similarity2
Nucleotide bindingi95 – 100FADBy similarity6
Nucleotide bindingi352 – 354FADBy similarity3

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BioCyciARA:AT2G17420-MONOMER.
BRENDAi1.8.1.9. 399.

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin reductase 2 (EC:1.8.1.9)
Alternative name(s):
NADPH-dependent thioredoxin reductase 2
Short name:
NTR2
NADPH-dependent thioredoxin reductase A
Short name:
AtNTRA
Gene namesi
Name:NTR2
Synonyms:NTRA
Ordered Locus Names:At2g17420
ORF Names:F5J6.18
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G17420.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001667721 – 383Thioredoxin reductase 2Add BLAST383

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi197 ↔ 200Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ39242.
PRIDEiQ39242.

PTM databases

iPTMnetiQ39242.

Expressioni

Gene expression databases

GenevisibleiQ39242. AT.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi3702.AT2G17420.1.

Structurei

3D structure databases

ProteinModelPortaliQ39242.
SMRiQ39242.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiKOG0404. Eukaryota.
COG0492. LUCA.
HOGENOMiHOG000072912.
InParanoidiQ39242.
KOiK00384.
OrthoDBiEOG09360E6S.
PhylomeDBiQ39242.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR008255. Pyr_nucl-diS_OxRdtase_2_AS.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
IPR005982. Thioredox_Rdtase.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSiPR00469. PNDRDTASEII.
SUPFAMiSSF51905. SSF51905. 1 hit.
TIGRFAMsiTIGR01292. TRX_reduct. 1 hit.
PROSITEiPS00573. PYRIDINE_REDOX_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q39242-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCWISMSQSR FIIKSLFSTA GGFLLGSALS NPPSLATAFS SSSSSSSAAA
60 70 80 90 100
AVDMETHKTK VCIVGSGPAA HTAAIYASRA ELKPLLFEGW MANDIAPGGQ
110 120 130 140 150
LTTTTDVENF PGFPEGILGI DIVEKFRKQS ERFGTTIFTE TVNKVDFSSK
160 170 180 190 200
PFKLFTDSRT VLADSVIIST GAVAKRLSFT GSGEGNGGFW NRGISACAVC
210 220 230 240 250
DGAAPIFRNK PLVVIGGGDS AMEEANFLTK YGSKVYIIHR RDTFRASKIM
260 270 280 290 300
QQRALSNPKI EVIWNSAVVE AYGDENGRVL GGLKVKNVVT GDVSDLKVSG
310 320 330 340 350
LFFAIGHEPA TKFLDGQLEL DEDGYVVTKP GTTKTSVVGV FAAGDVQDKK
360 370 380
YRQAITAAGT GCMAALDAEH YLQEIGSQEG KSD
Length:383
Mass (Da):40,635
Last modified:December 1, 2000 - v2
Checksum:i1BA9339AE6E66FFE
GO

Sequence cautioni

The sequence AEC06623 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti89 – 90GW → PR in CAA80655 (PubMed:8308900).Curated2
Sequence conflicti308E → Q in CAA80655 (PubMed:8308900).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002685 Genomic DNA. Translation: AEC06623.1. Different initiation.
AK226480 mRNA. Translation: BAE98622.1.
Z23108 mRNA. Translation: CAA80655.1.
AY099756 mRNA. Translation: AAM20607.1.
PIRiA84552.
S44026.
RefSeqiNP_179334.5. NM_127297.5.
UniGeneiAt.24973.
At.67791.

Genome annotation databases

EnsemblPlantsiAT2G17420.1; AT2G17420.1; AT2G17420.
GeneIDi816248.
GrameneiAT2G17420.1; AT2G17420.1; AT2G17420.
KEGGiath:AT2G17420.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002685 Genomic DNA. Translation: AEC06623.1. Different initiation.
AK226480 mRNA. Translation: BAE98622.1.
Z23108 mRNA. Translation: CAA80655.1.
AY099756 mRNA. Translation: AAM20607.1.
PIRiA84552.
S44026.
RefSeqiNP_179334.5. NM_127297.5.
UniGeneiAt.24973.
At.67791.

3D structure databases

ProteinModelPortaliQ39242.
SMRiQ39242.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT2G17420.1.

PTM databases

iPTMnetiQ39242.

Proteomic databases

PaxDbiQ39242.
PRIDEiQ39242.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G17420.1; AT2G17420.1; AT2G17420.
GeneIDi816248.
GrameneiAT2G17420.1; AT2G17420.1; AT2G17420.
KEGGiath:AT2G17420.

Organism-specific databases

TAIRiAT2G17420.

Phylogenomic databases

eggNOGiKOG0404. Eukaryota.
COG0492. LUCA.
HOGENOMiHOG000072912.
InParanoidiQ39242.
KOiK00384.
OrthoDBiEOG09360E6S.
PhylomeDBiQ39242.

Enzyme and pathway databases

BioCyciARA:AT2G17420-MONOMER.
BRENDAi1.8.1.9. 399.

Miscellaneous databases

PROiQ39242.

Gene expression databases

GenevisibleiQ39242. AT.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR008255. Pyr_nucl-diS_OxRdtase_2_AS.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
IPR005982. Thioredox_Rdtase.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSiPR00469. PNDRDTASEII.
SUPFAMiSSF51905. SSF51905. 1 hit.
TIGRFAMsiTIGR01292. TRX_reduct. 1 hit.
PROSITEiPS00573. PYRIDINE_REDOX_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTRXB2_ARATH
AccessioniPrimary (citable) accession number: Q39242
Secondary accession number(s): F4INH1
, O22751, Q0WW76, Q8LPI1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 1, 2000
Last modified: November 30, 2016
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.By similarity

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.