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UniProtKB - Q25861 (TRXR_PLAF5)
Protein
Thioredoxin reductase
Gene
TRXR
Organism
Plasmodium falciparum (isolate FCH-5)
Status
Functioni
Catalyzes the transfer of electrons from NADPH to thioredoxins TRX1, TRX2 and TRX3, which in turn act as reductants of disulfide containing proteins (PubMed:8892299).
Able to reduce nitroglutathione (GSNO), a compound involved in the transport of nitric oxide (NO); however, TRX1 is more efficient in reducing GSNO. Has no catalytic activity towards oxidized glutathione (GSSG) (By similarity).
By similarity1 PublicationMiscellaneous
There are 2 isoforms resulting from alternative translation initiation. The displayed sequence is likely to represent the shorter isoform.Curated
In Plasmodium, the C-terminal redox center, which acts as the active site, is formed by two cysteines while in mammalian TRXR this redox center is composed of a cysteine-selenocysteine active site.By similarity
Caution
Was originally thought to be a glutathione reductase.1 Publication
Catalytic activityi
Cofactori
FADBy similarityNote: Binds 1 FAD per subunit.By similarity
Kineticsi
- KM=4.1 µM for NADPH (at 20 degrees Celsius and pH 7.4)1 Publication
- KM=66 µM for E.coli thioredoxin (at 37 degrees Celsius and pH 7.6)1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 161 | FAD; via amide nitrogen and carbonyl oxygenBy similarity | 1 | |
Binding sitei | 357 | FADBy similarity | 1 | |
Active sitei | 509 | Proton acceptorBy similarity | 1 | |
Binding sitei | 509 | FAD; via carbonyl oxygen; shared with dimeric partnerBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 51 – 52 | FADBy similarity | 2 | |
Nucleotide bindingi | 71 – 74 | FADBy similarity | 4 | |
Nucleotide bindingi | 87 – 88 | FADBy similarity | 2 | |
Nucleotide bindingi | 92 – 96 | FADBy similarity | 5 | |
Nucleotide bindingi | 364 – 366 | FADBy similarity | 3 |
GO - Molecular functioni
- flavin adenine dinucleotide binding Source: InterPro
- thioredoxin-disulfide reductase activity Source: UniProtKB-EC
GO - Biological processi
- cell redox homeostasis Source: InterPro
Keywordsi
Molecular function | Oxidoreductase |
Ligand | FAD, Flavoprotein, NADP |
Enzyme and pathway databases
SABIO-RKi | Q25861 |
Names & Taxonomyi
Protein namesi | Recommended name: Thioredoxin reductase1 Publication (EC:1.8.1.91 Publication)Short name: PfTrxR1 Publication |
Gene namesi | Name:TRXR1 Publication Synonyms:GR1 Publication |
Organismi | Plasmodium falciparum (isolate FCH-5) |
Taxonomic identifieri | 132416 [NCBI] |
Taxonomic lineagei | Eukaryota › Sar › Alveolata › Apicomplexa › Aconoidasida › Haemosporida › Plasmodiidae › Plasmodium › Plasmodium (Laverania) › |
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm By similarity
Other locations
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
CytoplasmPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000067986 | 1 – 541 | Thioredoxin reductaseAdd BLAST | 541 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 88 ↔ 93 | Redox-activeBy similarity | ||
Disulfide bondi | 535 ↔ 540 | Redox-activeBy similarity |
Keywords - PTMi
Disulfide bondInteractioni
Subunit structurei
Homodimer.
1 PublicationFamily & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 438 – 452 | Loop important for the interaction with TRX1By similarityAdd BLAST | 15 |
Sequence similaritiesi
Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.Curated
Keywords - Domaini
Redox-active centerFamily and domain databases
Gene3Di | 3.50.50.60, 1 hit |
InterProi | View protein in InterPro IPR036188, FAD/NAD-bd_sf IPR023753, FAD/NAD-binding_dom IPR016156, FAD/NAD-linked_Rdtase_dimer_sf IPR001100, Pyr_nuc-diS_OxRdtase IPR004099, Pyr_nucl-diS_OxRdtase_dimer IPR012999, Pyr_OxRdtase_I_AS IPR006338, Thioredoxin/glutathione_Rdtase |
Pfami | View protein in Pfam PF07992, Pyr_redox_2, 1 hit PF02852, Pyr_redox_dim, 1 hit |
PIRSFi | PIRSF000350, Mercury_reductase_MerA, 1 hit |
SUPFAMi | SSF51905, SSF51905, 1 hit SSF55424, SSF55424, 1 hit |
TIGRFAMsi | TIGR01438, TGR, 1 hit |
PROSITEi | View protein in PROSITE PS00076, PYRIDINE_REDOX_1, 1 hit |
i Sequence
Sequence statusi: Complete.
Q25861-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MCKDKNEKKN YEHVNANEKN GYLASEKNEL TKNKVEEHTY DYDYVVIGGG
60 70 80 90 100
PGGMASAKEA AAHGARVLLF DYVKPSSQGT KWGIGGTCVN VGCVPKKLMH
110 120 130 140 150
YAGHMGSIFK LDSKAYGWKF DNLKHDWKKL VTTVQSHIRS LNFSYMTGLR
160 170 180 190 200
SSKVKYINGL AKLKDKNTVS YYLKGDLSKE ETVTGKYILI ATGCRPHIPD
210 220 230 240 250
DVEGAKELSI TSDDIFSLKK DPGKTLVVGA SYVALECSGF LNSLGYDVTV
260 270 280 290 300
AVRSIVLRGF DQQCAVKVKL YMEEQGVMFK NGILPKKLTK MDDKILVEFS
310 320 330 340 350
DKTSELYDTV LYAIGRKGDI DGLNLESLNM NVNKSNNKII ADHLSCTNIP
360 370 380 390 400
SIFAVGDVAE NVPELAPVAI KAGEILARRL FKDSDEIMDY SYIPTSIYTP
410 420 430 440 450
IEYGACGYSE EKAYELYGKS NVEVFLQEFN NLEISAVHRQ KHIRAQKDEY
460 470 480 490 500
DLDVSSTCLA KLVCLKNEDN RVIGFHYVGP NAGEVTQGMA LALRLKVKKK
510 520 530 540
DFDNCIGIHP TDAESFMNLF VTISSGLSYA AKGGCGGGKC G
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 49 – 51 | GGP → AGS in CAA58583 (PubMed:8892299).Curated | 3 | |
Sequence conflicti | 512 – 517 | DAESFM → AAEELS in CAA58583 (PubMed:8892299).Curated | 6 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X87095 mRNA Translation: CAA60574.1 X83603 Genomic DNA Translation: CAA58583.1 |
PIRi | S57658 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X87095 mRNA Translation: CAA60574.1 X83603 Genomic DNA Translation: CAA58583.1 |
PIRi | S57658 |
3D structure databases
AlphaFoldDBi | Q25861 |
SMRi | Q25861 |
ModBasei | Search... |
Enzyme and pathway databases
SABIO-RKi | Q25861 |
Family and domain databases
Gene3Di | 3.50.50.60, 1 hit |
InterProi | View protein in InterPro IPR036188, FAD/NAD-bd_sf IPR023753, FAD/NAD-binding_dom IPR016156, FAD/NAD-linked_Rdtase_dimer_sf IPR001100, Pyr_nuc-diS_OxRdtase IPR004099, Pyr_nucl-diS_OxRdtase_dimer IPR012999, Pyr_OxRdtase_I_AS IPR006338, Thioredoxin/glutathione_Rdtase |
Pfami | View protein in Pfam PF07992, Pyr_redox_2, 1 hit PF02852, Pyr_redox_dim, 1 hit |
PIRSFi | PIRSF000350, Mercury_reductase_MerA, 1 hit |
SUPFAMi | SSF51905, SSF51905, 1 hit SSF55424, SSF55424, 1 hit |
TIGRFAMsi | TIGR01438, TGR, 1 hit |
PROSITEi | View protein in PROSITE PS00076, PYRIDINE_REDOX_1, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | TRXR_PLAF5 | |
Accessioni | Q25861Primary (citable) accession number: Q25861 Secondary accession number(s): Q25864 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | December 1, 2000 |
Last sequence update: | November 1, 1996 | |
Last modified: | May 25, 2022 | |
This is version 132 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) |