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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)DescriptionActionsGraphical viewLength
Binding sitei101FAD1 Publication1
Binding sitei134FAD; via amide nitrogen and carbonyl oxygen1 Publication1
Binding sitei192FAD1 Publication1
Binding sitei337FAD1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi58 – 61FAD1 Publication4
Nucleotide bindingi79 – 80FAD1 Publication2
Nucleotide bindingi87 – 92FAD1 Publication6
Nucleotide bindingi344 – 346FAD1 Publication3

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001667711 – 375Thioredoxin reductase 1Add BLAST375

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

1375
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi47 – 56Combined sources10
Helixi60 – 71Combined sources12
Beta strandi77 – 79Combined sources3
Beta strandi82 – 84Combined sources3
Helixi92 – 95Combined sources4
Beta strandi97 – 99Combined sources3
Helixi111 – 124Combined sources14
Beta strandi128 – 130Combined sources3
Beta strandi136 – 138Combined sources3
Beta strandi140 – 147Combined sources8
Beta strandi149 – 160Combined sources12
Beta strandi164 – 166Combined sources3
Beta strandi175 – 179Combined sources5
Turni183 – 185Combined sources3
Beta strandi186 – 188Combined sources3
Helixi190 – 193Combined sources4
Helixi197 – 199Combined sources3
Beta strandi202 – 207Combined sources6
Helixi211 – 220Combined sources10
Turni221 – 223Combined sources3
Beta strandi224 – 230Combined sources7
Beta strandi232 – 235Combined sources4
Helixi240 – 247Combined sources8
Beta strandi252 – 255Combined sources4
Beta strandi257 – 279Combined sources23
Turni280 – 282Combined sources3
Beta strandi285 – 289Combined sources5
Beta strandi291 – 295Combined sources5
Beta strandi299 – 302Combined sources4
Helixi304 – 306Combined sources3
Beta strandi332 – 334Combined sources3
Helixi336 – 339Combined sources4
Helixi346 – 366Combined sources21

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VDCX-ray2.50A43-375[»]
ProteinModelPortaliQ39243.
SMRiQ39243.
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)DescriptionActionsGraphical viewLength
Sequence conflicti255I → F in AAO42318 (PubMed:14593172).Curated1

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_119711.4.
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_119711.4.
UniGeneiAt.3705.
At.69236.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VDCX-ray2.50A43-375[»]
ProteinModelPortaliQ39243.
SMRiQ39243.
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: November 30, 2016
This is version 138 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.