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Protein

Thioredoxin reductase

Gene

trxB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.

Cofactori

FAD1 PublicationNote: Binds 1 FAD per subunit.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi36 – 43FAD1 Publication8
Nucleotide bindingi287 – 296FAD1 Publication10

GO - Molecular functioni

  • flavin adenine dinucleotide binding Source: EcoCyc
  • thioredoxin-disulfide reductase activity Source: CACAO

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BioCyciEcoCyc:THIOREDOXIN-REDUCT-NADPH-MONOMER.
ECOL316407:JW0871-MONOMER.
MetaCyc:THIOREDOXIN-REDUCT-NADPH-MONOMER.
BRENDAi1.8.1.9. 2026.
SABIO-RKP0A9P4.

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin reductase (EC:1.8.1.9)
Short name:
TRXR
Gene namesi
Name:trxB
Ordered Locus Names:b0888, JW0871
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11032. trxB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3638339.
DrugBankiDB03147. Flavin adenine dinucleotide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001667292 – 321Thioredoxin reductaseAdd BLAST320

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi136 ↔ 139Redox-active1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiP0A9P4.
PaxDbiP0A9P4.
PRIDEiP0A9P4.

2D gel databases

SWISS-2DPAGEP0A9P4.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
trxAP0AA252EBI-1029826,EBI-368542

Protein-protein interaction databases

BioGridi4261715. 36 interactors.
DIPiDIP-6168N.
IntActiP0A9P4. 15 interactors.
STRINGi511145.b0888.

Chemistry databases

BindingDBiP0A9P4.

Structurei

Secondary structure

1321
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 12Combined sources9
Helixi16 – 26Combined sources11
Turni27 – 29Combined sources3
Beta strandi33 – 35Combined sources3
Helixi42 – 46Combined sources5
Helixi62 – 75Combined sources14
Beta strandi79 – 81Combined sources3
Beta strandi85 – 89Combined sources5
Beta strandi91 – 101Combined sources11
Beta strandi103 – 111Combined sources9
Beta strandi115 – 117Combined sources3
Helixi123 – 127Combined sources5
Turni130 – 132Combined sources3
Beta strandi133 – 135Combined sources3
Helixi137 – 140Combined sources4
Helixi141 – 144Combined sources4
Beta strandi147 – 152Combined sources6
Helixi156 – 165Combined sources10
Turni166 – 168Combined sources3
Beta strandi169 – 175Combined sources7
Beta strandi177 – 180Combined sources4
Helixi185 – 196Combined sources12
Beta strandi198 – 203Combined sources6
Beta strandi207 – 213Combined sources7
Beta strandi215 – 224Combined sources10
Beta strandi227 – 229Combined sources3
Beta strandi233 – 236Combined sources4
Beta strandi238 – 242Combined sources5
Beta strandi246 – 249Combined sources4
Helixi251 – 253Combined sources3
Turni254 – 256Combined sources3
Beta strandi269 – 272Combined sources4
Beta strandi282 – 284Combined sources3
Helixi286 – 289Combined sources4
Beta strandi291 – 293Combined sources3
Helixi296 – 314Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CL0X-ray2.50A2-321[»]
1F6MX-ray2.95A/B/E/F2-321[»]
1TDEX-ray2.10A2-317[»]
1TDFX-ray2.30A2-317[»]
1TRBX-ray2.00A2-321[»]
ProteinModelPortaliP0A9P4.
SMRiP0A9P4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A9P4.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiENOG4105C3M. Bacteria.
COG0492. LUCA.
HOGENOMiHOG000072912.
InParanoidiP0A9P4.
KOiK00384.
OMAiGQLEMNN.
PhylomeDBiP0A9P4.

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.

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

P0A9P4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGTTKHSKLL ILGSGPAGYT AAVYAARANL QPVLITGMEK GGQLTTTTEV
60 70 80 90 100
ENWPGDPNDL TGPLLMERMH EHATKFETEI IFDHINKVDL QNRPFRLNGD
110 120 130 140 150
NGEYTCDALI IATGASARYL GLPSEEAFKG RGVSACATCD GFFYRNQKVA
160 170 180 190 200
VIGGGNTAVE EALYLSNIAS EVHLIHRRDG FRAEKILIKR LMDKVENGNI
210 220 230 240 250
ILHTNRTLEE VTGDQMGVTG VRLRDTQNSD NIESLDVAGL FVAIGHSPNT
260 270 280 290 300
AIFEGQLELE NGYIKVQSGI HGNATQTSIP GVFAAGDVMD HIYRQAITSA
310 320
GTGCMAALDA ERYLDGLADA K
Length:321
Mass (Da):34,623
Last modified:January 23, 2007 - v2
Checksum:i8E5AF86FB195CC82
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03762 Genomic DNA. Translation: AAA24697.1.
U00096 Genomic DNA. Translation: AAC73974.1.
AP009048 Genomic DNA. Translation: BAA35613.1.
L21749 Genomic DNA. Translation: AAA66170.1.
M95935 Genomic DNA. No translation available.
PIRiA28074. RDECT.
RefSeqiNP_415408.1. NC_000913.3.
WP_000537418.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73974; AAC73974; b0888.
BAA35613; BAA35613; BAA35613.
GeneIDi949054.
KEGGiecj:JW0871.
eco:b0888.
PATRICi32116985. VBIEscCol129921_0917.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03762 Genomic DNA. Translation: AAA24697.1.
U00096 Genomic DNA. Translation: AAC73974.1.
AP009048 Genomic DNA. Translation: BAA35613.1.
L21749 Genomic DNA. Translation: AAA66170.1.
M95935 Genomic DNA. No translation available.
PIRiA28074. RDECT.
RefSeqiNP_415408.1. NC_000913.3.
WP_000537418.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CL0X-ray2.50A2-321[»]
1F6MX-ray2.95A/B/E/F2-321[»]
1TDEX-ray2.10A2-317[»]
1TDFX-ray2.30A2-317[»]
1TRBX-ray2.00A2-321[»]
ProteinModelPortaliP0A9P4.
SMRiP0A9P4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261715. 36 interactors.
DIPiDIP-6168N.
IntActiP0A9P4. 15 interactors.
STRINGi511145.b0888.

Chemistry databases

BindingDBiP0A9P4.
ChEMBLiCHEMBL3638339.
DrugBankiDB03147. Flavin adenine dinucleotide.

2D gel databases

SWISS-2DPAGEP0A9P4.

Proteomic databases

EPDiP0A9P4.
PaxDbiP0A9P4.
PRIDEiP0A9P4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73974; AAC73974; b0888.
BAA35613; BAA35613; BAA35613.
GeneIDi949054.
KEGGiecj:JW0871.
eco:b0888.
PATRICi32116985. VBIEscCol129921_0917.

Organism-specific databases

EchoBASEiEB1025.
EcoGeneiEG11032. trxB.

Phylogenomic databases

eggNOGiENOG4105C3M. Bacteria.
COG0492. LUCA.
HOGENOMiHOG000072912.
InParanoidiP0A9P4.
KOiK00384.
OMAiGQLEMNN.
PhylomeDBiP0A9P4.

Enzyme and pathway databases

BioCyciEcoCyc:THIOREDOXIN-REDUCT-NADPH-MONOMER.
ECOL316407:JW0871-MONOMER.
MetaCyc:THIOREDOXIN-REDUCT-NADPH-MONOMER.
BRENDAi1.8.1.9. 2026.
SABIO-RKP0A9P4.

Miscellaneous databases

EvolutionaryTraceiP0A9P4.
PROiP0A9P4.

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 nameiTRXB_ECOLI
AccessioniPrimary (citable) accession number: P0A9P4
Secondary accession number(s): P09625
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  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.