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Protein

Thioredoxin-1

Gene

trxA

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

Functioni

Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei27Deprotonates C-terminal active site Cys1
Active sitei33Nucleophile1
Sitei34Contributes to redox potential value1
Sitei35Contributes to redox potential value1
Active sitei36Nucleophile1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Host-virus interaction, Transport

Enzyme and pathway databases

BioCyciEcoCyc:RED-THIOREDOXIN-MONOMER.
ECOL316407:JW5856-MONOMER.
MetaCyc:RED-THIOREDOXIN-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin-1
Short name:
Trx-1
Gene namesi
Name:trxA
Synonyms:fipA, tsnC
Ordered Locus Names:b3781, JW5856
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11031. trxA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001200962 – 109Thioredoxin-1Add BLAST108

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi33 ↔ 36Redox-activePROSITE-ProRule annotation1 Publication
Modified residuei70N6-acetyllysine1 Publication1

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

EPDiP0AA25.
PaxDbiP0AA25.
PRIDEiP0AA25.

2D gel databases

SWISS-2DPAGEP0AA25.

Interactioni

Subunit structurei

Monomer. Interacts with bacteriophage T3 DNA polymerase.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
At2g44920O221602EBI-368542,EBI-2895776From a different organism.
FKBP13Q9SCY22EBI-368542,EBI-2895757From a different organism.
PPD6Q9LXX52EBI-368542,EBI-2895738From a different organism.
PRXQQ9LU862EBI-368542,EBI-540311From a different organism.
PSBO1P233212EBI-368542,EBI-449414From a different organism.
PSBO2Q9S8412EBI-368542,EBI-449424From a different organism.
TL17P817602EBI-368542,EBI-449573From a different organism.
TL29P822812EBI-368542,EBI-2895799From a different organism.
trxBP0A9P42EBI-368542,EBI-1029826
VDE1Q392492EBI-368542,EBI-2895666From a different organism.

Protein-protein interaction databases

BioGridi4263316. 272 interactors.
DIPiDIP-31856N.
IntActiP0AA25. 98 interactors.
MINTiMINT-1530752.
STRINGi511145.b3781.

Structurei

Secondary structure

1109
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 8Combined sources4
Turni10 – 12Combined sources3
Helixi13 – 16Combined sources4
Turni17 – 19Combined sources3
Beta strandi22 – 29Combined sources8
Helixi34 – 49Combined sources16
Turni50 – 53Combined sources4
Beta strandi55 – 60Combined sources6
Turni61 – 63Combined sources3
Helixi65 – 70Combined sources6
Beta strandi75 – 83Combined sources9
Beta strandi86 – 93Combined sources8
Helixi97 – 105Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F6MX-ray2.95C/D/G/H2-109[»]
1KEBX-ray1.80A/B2-109[»]
1M7TNMR-A32-108[»]
1OAZX-ray2.78A/B2-109[»]
1SKRX-ray2.40B2-109[»]
1SKSX-ray2.30B2-109[»]
1SKWX-ray2.30B2-109[»]
1SL0X-ray3.20B/D2-109[»]
1SL1X-ray2.20B2-109[»]
1SL2X-ray2.30B2-109[»]
1SRXX-ray2.80A2-109[»]
1T7PX-ray2.20B2-109[»]
1T8EX-ray2.54B2-109[»]
1THOX-ray2.30A2-109[»]
1TK0X-ray2.30B2-109[»]
1TK5X-ray2.20B2-109[»]
1TK8X-ray2.50B2-109[»]
1TKDX-ray2.49B2-109[»]
1TXXX-ray2.20A2-109[»]
1X9MX-ray2.10B2-109[»]
1X9SX-ray2.70B2-109[»]
1X9WX-ray2.30B2-109[»]
1XOANMR-A2-109[»]
1XOBNMR-A2-109[»]
1ZCPX-ray2.30A/B/C/D2-109[»]
1ZYQX-ray2.70B2-109[»]
1ZZYX-ray2.50A/B2-109[»]
2AJQX-ray2.60B/I2-109[»]
2BTOX-ray2.50T2-109[»]
2EIOX-ray2.60A/B/C/D2-109[»]
2EIQX-ray1.90A/B2-109[»]
2EIRX-ray2.50A/B/C/D2-109[»]
2FCHX-ray2.60A/B/C/D/E/F/G2-109[»]
2FD3X-ray2.45A/B2-109[»]
2H6XX-ray2.60A/B2-109[»]
2H6YX-ray2.40A/B2-109[»]
2H6ZX-ray2.25A/B2-109[»]
2H70X-ray2.70A/B2-109[»]
2H71X-ray2.20A/B2-109[»]
2H72X-ray2.25A/B2-109[»]
2H73X-ray2.45A/B2-109[»]
2H74X-ray2.40A/B4-109[»]
2H75X-ray2.20A/B2-109[»]
2H76X-ray2.25A/B2-109[»]
2O8VX-ray3.00B2-109[»]
2TIRX-ray2.00A2-109[»]
2TRXX-ray1.68A/B2-109[»]
3DYRX-ray2.00A/B2-109[»]
4HU7X-ray1.40A/B2-109[»]
4HU9X-ray1.55A2-109[»]
4HUAX-ray1.10A2-109[»]
4X43X-ray1.65A/B/C2-109[»]
ProteinModelPortaliP0AA25.
SMRiP0AA25.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AA25.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 109ThioredoxinPROSITE-ProRule annotationAdd BLAST108

Sequence similaritiesi

Belongs to the thioredoxin family.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG0526. LUCA.
HOGENOMiHOG000292977.
InParanoidiP0AA25.
KOiK03671.
OMAiMSEHIHY.
PhylomeDBiP0AA25.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR10438. PTHR10438. 1 hit.
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
PIRSFiPIRSF000077. Thioredoxin. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR01068. thioredoxin. 1 hit.
PROSITEiPS00194. 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.

P0AA25-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDKIIHLTD DSFDTDVLKA DGAILVDFWA EWCGPCKMIA PILDEIADEY
60 70 80 90 100
QGKLTVAKLN IDQNPGTAPK YGIRGIPTLL LFKNGEVAAT KVGALSKGQL

KEFLDANLA
Length:109
Mass (Da):11,807
Last modified:January 23, 2007 - v2
Checksum:iEF5933EA29668EE9
GO

Sequence cautioni

The sequence AAA24534 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAA67582 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti72 – 73GI → IG AA sequence (PubMed:4883076).Curated2
Sequence conflicti88A → AS in AAA24696 (PubMed:1379743).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M26133 Genomic DNA. Translation: AAA24693.1.
K02845 Genomic DNA. Translation: AAA24534.1. Different initiation.
M10424 Genomic DNA. Translation: AAA24533.1.
M54881 Genomic DNA. Translation: AAA24696.1.
M12779 Genomic DNA. Translation: AAA24694.1.
M87049 Genomic DNA. Translation: AAA67582.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76786.2.
AP009048 Genomic DNA. Translation: BAE77517.1.
PIRiA91519. TXEC.
RefSeqiNP_418228.2. NC_000913.3.
WP_001280776.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76786; AAC76786; b3781.
BAE77517; BAE77517; BAE77517.
GeneIDi23335415.
948289.
KEGGiecj:JW5856.
eco:b3781.
PATRICi32123053. VBIEscCol129921_3896.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M26133 Genomic DNA. Translation: AAA24693.1.
K02845 Genomic DNA. Translation: AAA24534.1. Different initiation.
M10424 Genomic DNA. Translation: AAA24533.1.
M54881 Genomic DNA. Translation: AAA24696.1.
M12779 Genomic DNA. Translation: AAA24694.1.
M87049 Genomic DNA. Translation: AAA67582.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76786.2.
AP009048 Genomic DNA. Translation: BAE77517.1.
PIRiA91519. TXEC.
RefSeqiNP_418228.2. NC_000913.3.
WP_001280776.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F6MX-ray2.95C/D/G/H2-109[»]
1KEBX-ray1.80A/B2-109[»]
1M7TNMR-A32-108[»]
1OAZX-ray2.78A/B2-109[»]
1SKRX-ray2.40B2-109[»]
1SKSX-ray2.30B2-109[»]
1SKWX-ray2.30B2-109[»]
1SL0X-ray3.20B/D2-109[»]
1SL1X-ray2.20B2-109[»]
1SL2X-ray2.30B2-109[»]
1SRXX-ray2.80A2-109[»]
1T7PX-ray2.20B2-109[»]
1T8EX-ray2.54B2-109[»]
1THOX-ray2.30A2-109[»]
1TK0X-ray2.30B2-109[»]
1TK5X-ray2.20B2-109[»]
1TK8X-ray2.50B2-109[»]
1TKDX-ray2.49B2-109[»]
1TXXX-ray2.20A2-109[»]
1X9MX-ray2.10B2-109[»]
1X9SX-ray2.70B2-109[»]
1X9WX-ray2.30B2-109[»]
1XOANMR-A2-109[»]
1XOBNMR-A2-109[»]
1ZCPX-ray2.30A/B/C/D2-109[»]
1ZYQX-ray2.70B2-109[»]
1ZZYX-ray2.50A/B2-109[»]
2AJQX-ray2.60B/I2-109[»]
2BTOX-ray2.50T2-109[»]
2EIOX-ray2.60A/B/C/D2-109[»]
2EIQX-ray1.90A/B2-109[»]
2EIRX-ray2.50A/B/C/D2-109[»]
2FCHX-ray2.60A/B/C/D/E/F/G2-109[»]
2FD3X-ray2.45A/B2-109[»]
2H6XX-ray2.60A/B2-109[»]
2H6YX-ray2.40A/B2-109[»]
2H6ZX-ray2.25A/B2-109[»]
2H70X-ray2.70A/B2-109[»]
2H71X-ray2.20A/B2-109[»]
2H72X-ray2.25A/B2-109[»]
2H73X-ray2.45A/B2-109[»]
2H74X-ray2.40A/B4-109[»]
2H75X-ray2.20A/B2-109[»]
2H76X-ray2.25A/B2-109[»]
2O8VX-ray3.00B2-109[»]
2TIRX-ray2.00A2-109[»]
2TRXX-ray1.68A/B2-109[»]
3DYRX-ray2.00A/B2-109[»]
4HU7X-ray1.40A/B2-109[»]
4HU9X-ray1.55A2-109[»]
4HUAX-ray1.10A2-109[»]
4X43X-ray1.65A/B/C2-109[»]
ProteinModelPortaliP0AA25.
SMRiP0AA25.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263316. 272 interactors.
DIPiDIP-31856N.
IntActiP0AA25. 98 interactors.
MINTiMINT-1530752.
STRINGi511145.b3781.

2D gel databases

SWISS-2DPAGEP0AA25.

Proteomic databases

EPDiP0AA25.
PaxDbiP0AA25.
PRIDEiP0AA25.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76786; AAC76786; b3781.
BAE77517; BAE77517; BAE77517.
GeneIDi23335415.
948289.
KEGGiecj:JW5856.
eco:b3781.
PATRICi32123053. VBIEscCol129921_3896.

Organism-specific databases

EchoBASEiEB1024.
EcoGeneiEG11031. trxA.

Phylogenomic databases

eggNOGiCOG0526. LUCA.
HOGENOMiHOG000292977.
InParanoidiP0AA25.
KOiK03671.
OMAiMSEHIHY.
PhylomeDBiP0AA25.

Enzyme and pathway databases

BioCyciEcoCyc:RED-THIOREDOXIN-MONOMER.
ECOL316407:JW5856-MONOMER.
MetaCyc:RED-THIOREDOXIN-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AA25.
PROiP0AA25.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR10438. PTHR10438. 1 hit.
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
PIRSFiPIRSF000077. Thioredoxin. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR01068. thioredoxin. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTHIO_ECOLI
AccessioniPrimary (citable) accession number: P0AA25
Secondary accession number(s): P00274
, P76750, Q2M889, Q47674, Q8XAT2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.