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Protein

Thioredoxin reductase 1

Gene

NTR1

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

Functioni

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

Catalytic activityi

Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.

Cofactori

FADNote: Binds 1 FAD per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei101 – 1011FAD1 Publication
Binding sitei134 – 1341FAD; via amide nitrogen and carbonyl oxygen1 Publication
Binding sitei192 – 1921FAD1 Publication
Binding sitei337 – 3371FAD1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi58 – 614FAD1 Publication
Nucleotide bindingi79 – 802FAD1 Publication
Nucleotide bindingi87 – 926FAD1 Publication
Nucleotide bindingi344 – 3463FAD1 Publication

GO - Molecular functioni

  • thioredoxin-disulfide reductase activity Source: TAIR

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:AT4G35460-MONOMER.
BRENDAi1.8.1.9. 399.

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin reductase 1 (EC:1.8.1.9)
Alternative name(s):
NADPH-dependent thioredoxin reductase 1
Short name:
NTR1
NADPH-dependent thioredoxin reductase B
Short name:
AtNTRB
Gene namesi
Name:NTR1
Synonyms:NTRB
Ordered Locus Names:At4g35460
ORF Names:F15J1.30
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G35460.

Subcellular locationi

GO - Cellular componenti

  • chloroplast envelope Source: TAIR
  • cytosol Source: TAIR
  • mitochondrion Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 375375Thioredoxin reductase 1PRO_0000166771Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi189 ↔ 192Redox-active1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ39243.
PRIDEiQ39243.

PTM databases

iPTMnetiQ39243.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

GenevisibleiQ39243. AT.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi3702.AT4G35460.1.

Structurei

Secondary structure

1
375
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi47 – 5610Combined sources
Helixi60 – 7112Combined sources
Beta strandi77 – 793Combined sources
Beta strandi82 – 843Combined sources
Helixi92 – 954Combined sources
Beta strandi97 – 993Combined sources
Helixi111 – 12414Combined sources
Beta strandi128 – 1303Combined sources
Beta strandi136 – 1383Combined sources
Beta strandi140 – 1478Combined sources
Beta strandi149 – 16012Combined sources
Beta strandi164 – 1663Combined sources
Beta strandi175 – 1795Combined sources
Turni183 – 1853Combined sources
Beta strandi186 – 1883Combined sources
Helixi190 – 1934Combined sources
Helixi197 – 1993Combined sources
Beta strandi202 – 2076Combined sources
Helixi211 – 22010Combined sources
Turni221 – 2233Combined sources
Beta strandi224 – 2307Combined sources
Beta strandi232 – 2354Combined sources
Helixi240 – 2478Combined sources
Beta strandi252 – 2554Combined sources
Beta strandi257 – 27923Combined sources
Turni280 – 2823Combined sources
Beta strandi285 – 2895Combined sources
Beta strandi291 – 2955Combined sources
Beta strandi299 – 3024Combined sources
Helixi304 – 3063Combined sources
Beta strandi332 – 3343Combined sources
Helixi336 – 3394Combined sources
Helixi346 – 36621Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VDCX-ray2.50A43-375[»]
ProteinModelPortaliQ39243.
SMRiQ39243. Positions 46-367.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ39243.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiKOG0404. Eukaryota.
COG0492. LUCA.
HOGENOMiHOG000072912.
InParanoidiQ39243.
KOiK00384.
OMAiTDSGQVW.
OrthoDBiEOG09360E6S.
PhylomeDBiQ39243.

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.

Q39243-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNCVSRLKCL ISKARSFARL GGESTLSQPP SLASAAFSSS AVMNGLETHN
60 70 80 90 100
TRLCIVGSGP AAHTAAIYAA RAELKPLLFE GWMANDIAPG GQLTTTTDVE
110 120 130 140 150
NFPGFPEGIL GVELTDKFRK QSERFGTTIF TETVTKVDFS SKPFKLFTDS
160 170 180 190 200
KAILADAVIL ATGAVAKRLS FVGSGEASGG FWNRGISACA VCDGAAPIFR
210 220 230 240 250
NKPLAVIGGG DSAMEEANFL TKYGSKVYII HRRDAFRASK IMQQRALSNP
260 270 280 290 300
KIDVIWNSSV VEAYGDGERD VLGGLKVKNV VTGDVSDLKV SGLFFAIGHE
310 320 330 340 350
PATKFLDGGV ELDSDGYVVT KPGTTQTSVP GVFAAGDVQD KKYRQAITAA
360 370
GTGCMAALDA EHYLQEIGSQ QGKSD
Length:375
Mass (Da):39,626
Last modified:June 15, 2010 - v3
Checksum:iF86B7FF70340C952
GO

Sequence cautioni

The sequence AAO42318 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAA80656 differs from that shown.Sequencing errors.Curated
The sequence CAB54874 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAB80262 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti255 – 2551I → F in AAO42318 (PubMed:14593172).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z23109 mRNA. Translation: CAA80656.1. Sequence problems.
AL117188 Genomic DNA. Translation: CAB54874.1. Different initiation.
AL161587 Genomic DNA. Translation: CAB80262.1. Different initiation.
CP002687 Genomic DNA. Translation: AEE86518.1.
BT004322 mRNA. Translation: AAO42318.1. Different initiation.
PIRiS44027.
T41743.
RefSeqiNP_195271.2. NM_119711.3.
UniGeneiAt.3705.
At.69236.

Genome annotation databases

EnsemblPlantsiAT4G35460.1; AT4G35460.1; AT4G35460.
GeneIDi829698.
GrameneiAT4G35460.1; AT4G35460.1; AT4G35460.
KEGGiath:AT4G35460.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z23109 mRNA. Translation: CAA80656.1. Sequence problems.
AL117188 Genomic DNA. Translation: CAB54874.1. Different initiation.
AL161587 Genomic DNA. Translation: CAB80262.1. Different initiation.
CP002687 Genomic DNA. Translation: AEE86518.1.
BT004322 mRNA. Translation: AAO42318.1. Different initiation.
PIRiS44027.
T41743.
RefSeqiNP_195271.2. NM_119711.3.
UniGeneiAt.3705.
At.69236.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VDCX-ray2.50A43-375[»]
ProteinModelPortaliQ39243.
SMRiQ39243. Positions 46-367.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G35460.1.

PTM databases

iPTMnetiQ39243.

Proteomic databases

PaxDbiQ39243.
PRIDEiQ39243.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G35460.1; AT4G35460.1; AT4G35460.
GeneIDi829698.
GrameneiAT4G35460.1; AT4G35460.1; AT4G35460.
KEGGiath:AT4G35460.

Organism-specific databases

TAIRiAT4G35460.

Phylogenomic databases

eggNOGiKOG0404. Eukaryota.
COG0492. LUCA.
HOGENOMiHOG000072912.
InParanoidiQ39243.
KOiK00384.
OMAiTDSGQVW.
OrthoDBiEOG09360E6S.
PhylomeDBiQ39243.

Enzyme and pathway databases

BioCyciARA:AT4G35460-MONOMER.
BRENDAi1.8.1.9. 399.

Miscellaneous databases

EvolutionaryTraceiQ39243.
PROiQ39243.

Gene expression databases

GenevisibleiQ39243. 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 nameiTRXB1_ARATH
AccessioniPrimary (citable) accession number: Q39243
Secondary accession number(s): Q84W20, Q9SVW9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 15, 2010
Last modified: September 7, 2016
This is version 136 of the entry and version 3 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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.