SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P0AA25

- THIO_ECOLI

UniProt

P0AA25 - THIO_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Thioredoxin-1
Gene
trxA, fipA, tsnC, b3781, JW5856
Organism
Escherichia coli (strain K12)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Sitei27 – 271Deprotonates C-terminal active site Cys
Active sitei33 – 331Nucleophile
Sitei34 – 341Contributes to redox potential value
Sitei35 – 351Contributes to redox potential value
Active sitei36 – 361Nucleophile

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. protein disulfide oxidoreductase activity Source: EcoCyc

GO - Biological processi

  1. cell redox homeostasis Source: EcoCyc
  2. glycerol ether metabolic process Source: InterPro
  3. viral process Source: UniProtKB-KW
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11031. trxA.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 109108Thioredoxin-1
PRO_0000120096Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi33 ↔ 36Redox-active1 Publication
Modified residuei70 – 701N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

PaxDbiP0AA25.
PRIDEiP0AA25.

2D gel databases

SWISS-2DPAGEP0AA25.

Expressioni

Gene expression databases

GenevestigatoriP0AA25.

Interactioni

Subunit structurei

Monomer. Interacts with bacteriophage T3 DNA polymerase.

Binary interactionsi

WithEntry#Exp.IntActNotes
At2g44920O221602EBI-368542,EBI-2895776From a different organism.
At5g53490P817602EBI-368542,EBI-449573From 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.
TL29P822812EBI-368542,EBI-2895799From a different organism.
trxBP0A9P42EBI-368542,EBI-1029826
VDE1Q392492EBI-368542,EBI-2895666From a different organism.

Protein-protein interaction databases

DIPiDIP-31856N.
IntActiP0AA25. 98 interactions.
MINTiMINT-1530752.
STRINGi511145.b3781.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 84
Turni10 – 123
Helixi13 – 164
Turni17 – 193
Beta strandi22 – 298
Helixi34 – 4916
Turni50 – 534
Beta strandi55 – 606
Turni61 – 633
Helixi65 – 706
Beta strandi75 – 839
Beta strandi86 – 938
Helixi97 – 1059

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F6MX-ray2.95C/D/G/H2-109[»]
1KEBX-ray1.80A/B2-109[»]
1M7TNMR-A34-108[»]
1OAZX-ray2.77A/B1-109[»]
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[»]
ProteinModelPortaliP0AA25.
SMRiP0AA25. Positions 2-109.

Miscellaneous databases

EvolutionaryTraceiP0AA25.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 109108Thioredoxin
Add
BLAST

Sequence similaritiesi

Belongs to the thioredoxin family.
Contains 1 thioredoxin domain.

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG0526.
HOGENOMiHOG000292977.
KOiK03671.
OMAiIHITSAD.
OrthoDBiEOG6QG8RK.
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

MSDKIIHLTD DSFDTDVLKA DGAILVDFWA EWCGPCKMIA PILDEIADEY    50
QGKLTVAKLN IDQNPGTAPK YGIRGIPTLL LFKNGEVAAT KVGALSKGQL 100
KEFLDANLA 109
Length:109
Mass (Da):11,807
Last modified:January 23, 2007 - v2
Checksum:iEF5933EA29668EE9
GO

Sequence cautioni

The sequence AAA24534.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence AAA67582.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti72 – 732GI → IG AA sequence 1 Publication
Sequence conflicti88 – 881A → AS in AAA24696. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
YP_491658.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76786; AAC76786; b3781.
BAE77517; BAE77517; BAE77517.
GeneIDi12934322.
948289.
KEGGiecj:Y75_p3394.
eco:b3781.
PATRICi32123053. VBIEscCol129921_3896.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi A91519. TXEC.
RefSeqi NP_418228.2. NC_000913.3.
YP_491658.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1F6M X-ray 2.95 C/D/G/H 2-109 [» ]
1KEB X-ray 1.80 A/B 2-109 [» ]
1M7T NMR - A 34-108 [» ]
1OAZ X-ray 2.77 A/B 1-109 [» ]
1SKR X-ray 2.40 B 2-109 [» ]
1SKS X-ray 2.30 B 2-109 [» ]
1SKW X-ray 2.30 B 2-109 [» ]
1SL0 X-ray 3.20 B/D 2-109 [» ]
1SL1 X-ray 2.20 B 2-109 [» ]
1SL2 X-ray 2.30 B 2-109 [» ]
1SRX X-ray 2.80 A 2-109 [» ]
1T7P X-ray 2.20 B 2-109 [» ]
1T8E X-ray 2.54 B 2-109 [» ]
1THO X-ray 2.30 A 2-109 [» ]
1TK0 X-ray 2.30 B 2-109 [» ]
1TK5 X-ray 2.20 B 2-109 [» ]
1TK8 X-ray 2.50 B 2-109 [» ]
1TKD X-ray 2.49 B 2-109 [» ]
1TXX X-ray 2.20 A 2-109 [» ]
1X9M X-ray 2.10 B 2-109 [» ]
1X9S X-ray 2.70 B 2-109 [» ]
1X9W X-ray 2.30 B 2-109 [» ]
1XOA NMR - A 2-109 [» ]
1XOB NMR - A 2-109 [» ]
1ZCP X-ray 2.30 A/B/C/D 2-109 [» ]
1ZYQ X-ray 2.70 B 2-109 [» ]
1ZZY X-ray 2.50 A/B 2-109 [» ]
2AJQ X-ray 2.60 B/I 2-109 [» ]
2BTO X-ray 2.50 T 2-109 [» ]
2EIO X-ray 2.60 A/B/C/D 2-109 [» ]
2EIQ X-ray 1.90 A/B 2-109 [» ]
2EIR X-ray 2.50 A/B/C/D 2-109 [» ]
2FCH X-ray 2.60 A/B/C/D/E/F/G 2-109 [» ]
2FD3 X-ray 2.45 A/B 2-109 [» ]
2H6X X-ray 2.60 A/B 2-109 [» ]
2H6Y X-ray 2.40 A/B 2-109 [» ]
2H6Z X-ray 2.25 A/B 2-109 [» ]
2H70 X-ray 2.70 A/B 2-109 [» ]
2H71 X-ray 2.20 A/B 2-109 [» ]
2H72 X-ray 2.25 A/B 2-109 [» ]
2H73 X-ray 2.45 A/B 2-109 [» ]
2H74 X-ray 2.40 A/B 4-109 [» ]
2H75 X-ray 2.20 A/B 2-109 [» ]
2H76 X-ray 2.25 A/B 2-109 [» ]
2O8V X-ray 3.00 B 2-109 [» ]
2TIR X-ray 2.00 A 2-109 [» ]
2TRX X-ray 1.68 A/B 2-109 [» ]
3DYR X-ray 2.00 A/B 2-109 [» ]
4HU7 X-ray 1.40 A/B 2-109 [» ]
4HU9 X-ray 1.55 A 2-109 [» ]
4HUA X-ray 1.10 A 2-109 [» ]
ProteinModelPortali P0AA25.
SMRi P0AA25. Positions 2-109.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-31856N.
IntActi P0AA25. 98 interactions.
MINTi MINT-1530752.
STRINGi 511145.b3781.

2D gel databases

SWISS-2DPAGE P0AA25.

Proteomic databases

PaxDbi P0AA25.
PRIDEi P0AA25.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76786 ; AAC76786 ; b3781 .
BAE77517 ; BAE77517 ; BAE77517 .
GeneIDi 12934322.
948289.
KEGGi ecj:Y75_p3394.
eco:b3781.
PATRICi 32123053. VBIEscCol129921_3896.

Organism-specific databases

EchoBASEi EB1024.
EcoGenei EG11031. trxA.

Phylogenomic databases

eggNOGi COG0526.
HOGENOMi HOG000292977.
KOi K03671.
OMAi IHITSAD.
OrthoDBi EOG6QG8RK.
PhylomeDBi P0AA25.

Enzyme and pathway databases

BioCyci EcoCyc:RED-THIOREDOXIN-MONOMER.
ECOL316407:JW5856-MONOMER.
MetaCyc:RED-THIOREDOXIN-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0AA25.
PROi P0AA25.

Gene expression databases

Genevestigatori P0AA25.

Family and domain databases

Gene3Di 3.40.30.10. 1 hit.
InterProi IPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view ]
PANTHERi PTHR10438. PTHR10438. 1 hit.
Pfami PF00085. Thioredoxin. 1 hit.
[Graphical view ]
PIRSFi PIRSF000077. Thioredoxin. 1 hit.
SUPFAMi SSF52833. SSF52833. 1 hit.
TIGRFAMsi TIGR01068. thioredoxin. 1 hit.
PROSITEi PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Genetic and physical analysis of the thioredoxin (trxA) gene of Escherichia coli K-12."
    Wallace B.J., Kushner S.R.
    Gene 32:399-408(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Cloning and nucleotide sequence of the trxA gene of Escherichia coli K-12."
    Lim C.-J., Geraghty D., Fuchs J.A.
    J. Bacteriol. 163:311-316(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Physical analysis of the thioredoxin gene from Escherichia coli K-12."
    Wallace B.J., Zownir O., Kushner S.R.
    (In) Holmgren A. (eds.); Thioredoxin and glutaredoxin systems, structure and function, pp.11-19, Raven Press, New York (1986)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes."
    Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.
    Science 257:771-778(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  7. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  8. "Thioredoxin. 6. The amino acid sequence of the protein from Escherichia coli B."
    Holmgren A.
    Eur. J. Biochem. 6:475-484(1968) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-109.
    Strain: B.
  9. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  10. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
    Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
    Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
  11. "Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8-A resolution."
    Holmgren A., Soederberg B.-O., Eklund H., Braenden C.-I.
    Proc. Natl. Acad. Sci. U.S.A. 72:2305-2309(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
  12. "Structure of oxidized thioredoxin to 4 with 5-A resolution."
    Soederberg B.-O., Holmgren A., Braenden C.-I.
    J. Mol. Biol. 90:143-152(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (4.5 ANGSTROMS).
  13. "Crystal structure of thioredoxin from Escherichia coli at 1.68-A resolution."
    Katti S.K., le Master D.M., Eklund H.
    J. Mol. Biol. 212:167-184(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS).
  14. "Crystal structure analysis of a mutant Escherichia coli thioredoxin in which lysine 36 is replaced by glutamic acid."
    Nikkola M., Gleason F.K., Fuchs J.A., Eklund H.
    Biochemistry 32:5093-5098(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT GLU-37.
  15. "The CXXC motif: crystal structure of an active-site variant of Escherichia coli thioredoxin."
    Schultz L.W., Chivers P.T., Raines R.T.
    Acta Crystallogr. D 55:1533-1538(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), DISULFIDE BOND.
  16. "Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductase."
    Lennon B.W., Williams C.H. Jr., Ludwig M.L.
    Science 289:1190-1194(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH TRXB.
  17. "Three-dimensional solution structure of the reduced form of Escherichia coli thioredoxin determined by nuclear magnetic resonance spectroscopy."
    Dyson H.J., Gippert G.P., Case D.A., Holmgren A., Wright P.E.
    Biochemistry 29:4129-4136(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  18. "High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin."
    Jeng M.F., Campbell A.P., Begley T., Holmgren A., Case D.A., Wright P.E., Dyson H.J.
    Structure 2:853-868(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

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: September 3, 2014
This is version 96 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

External Data

Dasty 3

Similar proteinsi