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Protein

NADPH-dependent thioredoxin reductase 3

Gene

NTRC

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

Functioni

Thioredoxin reductase (TR) that exhibits both TR and thioredoxin (Trx) activities. Contains a C-terminal functional Trx domain. Functions as an electron donor for plastidial 2-Cys peroxiredoxins and participates in a NADPH-dependent hydrogen peroxide scavenging system in chloroplasts in the dark. Required for chlorophyll biosynthesis and biogenesis of the photosynthetic apparatus. Activates aerobic cyclase which converts Mg-protoporhyrin monomethyl ester into protochlorophyllide. Involved in a light-dependent regulation of starch biosynthesis by redox activation of the ADP-glucose pyrophosphorylase (AGPase), a central enzyme of starch synthesis.3 Publications

Catalytic activityi

Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.

Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei133FADBy similarity1
Binding sitei166FAD; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei220FADBy similarity1
Sitei241Important for activityBy similarity1
Sitei259Important for activityBy similarity1
Sitei260Important for activityBy similarity1
Binding sitei364FADBy similarity1
Active sitei454NucleophileBy similarity1
Active sitei457NucleophileBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi91 – 94FADBy similarity4
Nucleotide bindingi112 – 113FADBy similarity2
Nucleotide bindingi120 – 124FADBy similarity5
Nucleotide bindingi371 – 373FADBy similarity3

GO - Molecular functioni

  • enzyme activator activity Source: UniProtKB
  • oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor Source: UniProtKB
  • thioredoxin-disulfide reductase activity Source: UniProtKB

GO - Biological processi

  • cell redox homeostasis Source: UniProtKB
  • hydrogen peroxide catabolic process Source: TAIR
  • positive regulation of catalytic activity Source: UniProtKB
  • regulation of chlorophyll biosynthetic process Source: UniProtKB
  • regulation of starch biosynthetic process Source: UniProtKB
  • removal of superoxide radicals Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

FAD, Flavoprotein, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
NADPH-dependent thioredoxin reductase 3 (EC:1.8.1.9)
Short name:
NTR3
Alternative name(s):
NADPH-dependent thioredoxin reductase C
Short name:
ANTR-C
Short name:
AtNTRC
Gene namesi
Name:NTRC
Ordered Locus Names:At2g41680
ORF Names:T32G6.20
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G41680.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: UniProtKB
  • chloroplast stroma Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Disruption phenotypei

Dwarf plants with chlorotic leaves. Accumulation of Mg-protoporhyrin after feeding with 5-aminolevulinic acid.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 67ChloroplastSequence analysisAdd BLAST67
ChainiPRO_000039455268 – 529NADPH-dependent thioredoxin reductase 3Add BLAST462

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi217 ↔ 220Redox-activePROSITE-ProRule annotation
Disulfide bondi454 ↔ 457Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiO22229.

Expressioni

Gene expression databases

GenevisibleiO22229. AT.

Interactioni

Subunit structurei

May homodimerize. Interacts with the 2-Cys peroxiredoxin BAS1.1 Publication

Protein-protein interaction databases

BioGridi4103. 14 interactors.
IntActiO22229. 10 interactors.
STRINGi3702.AT2G41680.1.

Structurei

3D structure databases

ProteinModelPortaliO22229.
SMRiO22229.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini403 – 529ThioredoxinPROSITE-ProRule annotationAdd BLAST127

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi72 – 78Poly-Ser7

Sequence similaritiesi

Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

eggNOGiKOG0404. Eukaryota.
KOG0907. Eukaryota.
COG0492. LUCA.
COG0526. LUCA.
HOGENOMiHOG000072912.
InParanoidiO22229.
KOiK00384.
OMAiWSKGISA.
OrthoDBiEOG09360E6S.
PhylomeDBiO22229.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR008255. Pyr_nucl-diS_OxRdtase_2_AS.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
IPR005982. Thioredox_Rdtase.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF00085. Thioredoxin. 1 hit.
[Graphical view]
PRINTSiPR00469. PNDRDTASEII.
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR01292. TRX_reduct. 1 hit.
PROSITEiPS00573. PYRIDINE_REDOX_2. 1 hit.
PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O22229-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASPKIGIG IASVSSPHRV SAASSALSPP PHLFFLTTTT TTRHGGSYLL
60 70 80 90 100
RQPTRTRSSD SLRLRVSATA NSPSSSSSGG EIIENVVIIG SGPAGYTAAI
110 120 130 140 150
YAARANLKPV VFEGYQMGGV PGGQLMTTTE VENFPGFPDG ITGPDLMEKM
160 170 180 190 200
RKQAERWGAE LYPEDVESLS VTTAPFTVQT SERKVKCHSI IYATGATARR
210 220 230 240 250
LRLPREEEFW SRGISACAIC DGASPLFKGQ VLAVVGGGDT ATEEALYLTK
260 270 280 290 300
YARHVHLLVR RDQLRASKAM QDRVINNPNI TVHYNTETVD VLSNTKGQMS
310 320 330 340 350
GILLRRLDTG EETELEAKGL FYGIGHSPNS QLLEGQVELD SSGYVLVREG
360 370 380 390 400
TSNTSVEGVF AAGDVQDHEW RQAVTAAGSG CIAALSAERY LTSNNLLVEF
410 420 430 440 450
HQPQTEEAKK EFTQRDVQEK FDITLTKHKG QYALRKLYHE SPRVILVLYT
460 470 480 490 500
SPTCGPCRTL KPILNKVVDE YNHDVHFVEI DIEEDQEIAE AAGIMGTPCV
510 520
QFFKNKEMLR TISGVKMKKE YREFIEANK
Length:529
Mass (Da):57,950
Last modified:June 1, 2002 - v2
Checksum:i53853134652D64AA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti399E → K in AAN18085 (PubMed:14593172).Curated1
Sequence conflicti399E → K in AAL08250 (PubMed:14593172).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC002510 Genomic DNA. Translation: AAB84351.2.
CP002685 Genomic DNA. Translation: AEC10015.1.
AY056394 mRNA. Translation: AAL08250.1.
BT000516 mRNA. Translation: AAN18085.1.
AK229969 mRNA. Translation: BAF01794.1.
PIRiT00824.
RefSeqiNP_565954.1. NM_129731.6.
UniGeneiAt.12409.
At.42799.

Genome annotation databases

EnsemblPlantsiAT2G41680.1; AT2G41680.1; AT2G41680.
GeneIDi818766.
GrameneiAT2G41680.1; AT2G41680.1; AT2G41680.
KEGGiath:AT2G41680.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC002510 Genomic DNA. Translation: AAB84351.2.
CP002685 Genomic DNA. Translation: AEC10015.1.
AY056394 mRNA. Translation: AAL08250.1.
BT000516 mRNA. Translation: AAN18085.1.
AK229969 mRNA. Translation: BAF01794.1.
PIRiT00824.
RefSeqiNP_565954.1. NM_129731.6.
UniGeneiAt.12409.
At.42799.

3D structure databases

ProteinModelPortaliO22229.
SMRiO22229.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4103. 14 interactors.
IntActiO22229. 10 interactors.
STRINGi3702.AT2G41680.1.

Proteomic databases

PaxDbiO22229.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G41680.1; AT2G41680.1; AT2G41680.
GeneIDi818766.
GrameneiAT2G41680.1; AT2G41680.1; AT2G41680.
KEGGiath:AT2G41680.

Organism-specific databases

TAIRiAT2G41680.

Phylogenomic databases

eggNOGiKOG0404. Eukaryota.
KOG0907. Eukaryota.
COG0492. LUCA.
COG0526. LUCA.
HOGENOMiHOG000072912.
InParanoidiO22229.
KOiK00384.
OMAiWSKGISA.
OrthoDBiEOG09360E6S.
PhylomeDBiO22229.

Miscellaneous databases

PROiO22229.

Gene expression databases

GenevisibleiO22229. AT.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR008255. Pyr_nucl-diS_OxRdtase_2_AS.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
IPR005982. Thioredox_Rdtase.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF00085. Thioredoxin. 1 hit.
[Graphical view]
PRINTSiPR00469. PNDRDTASEII.
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR01292. TRX_reduct. 1 hit.
PROSITEiPS00573. PYRIDINE_REDOX_2. 1 hit.
PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTRXB3_ARATH
AccessioniPrimary (citable) accession number: O22229
Secondary accession number(s): Q0WM62, Q93ZQ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 1, 2002
Last modified: November 30, 2016
This is version 118 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.