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P0AA25 (THIO_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thioredoxin-1

Short name=Trx-1
Gene names
Name:trxA
Synonyms:fipA, tsnC
Ordered Locus Names:b3781, JW5856
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length109 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

Monomer. Interacts with bacteriophage T3 DNA polymerase.

Sequence similarities

Belongs to the thioredoxin family.

Contains 1 thioredoxin domain.

Sequence caution

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 109108Thioredoxin-1
PRO_0000120096

Regions

Domain2 – 109108Thioredoxin

Sites

Active site331Nucleophile
Active site361Nucleophile
Site271Deprotonates C-terminal active site Cys
Site341Contributes to redox potential value
Site351Contributes to redox potential value

Amino acid modifications

Modified residue701N6-acetyllysine Ref.10
Disulfide bond33 ↔ 36Redox-active Ref.15

Experimental info

Sequence conflict72 – 732GI → IG AA sequence Ref.8
Sequence conflict881A → AS in AAA24696. Ref.5

Secondary structure

....................... 109
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AA25 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: EF5933EA29668EE9

FASTA10911,807
        10         20         30         40         50         60 
MSDKIIHLTD DSFDTDVLKA DGAILVDFWA EWCGPCKMIA PILDEIADEY QGKLTVAKLN 

        70         80         90        100 
IDQNPGTAPK YGIRGIPTLL LFKNGEVAAT KVGALSKGQL KEFLDANLA 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the thioredoxin gene from Escherichia coli."
Hoeoeg J.-O., von Bahr-Lindstroem H., Josephson S., Wallace B.J., Kushner S.R., Joernvall H., Holmgren A.
Biosci. Rep. 4:917-923(1984) [PubMed] [Europe PMC] [Abstract]
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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRTXEC. A91519.
RefSeqNP_418228.2. NC_000913.3.
YP_491658.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F6MX-ray2.95C/D/G/H2-109[»]
1KEBX-ray1.80A/B2-108[»]
1M7TNMR-A68-108[»]
1OAZX-ray2.77A/B1-109[»]
1SKRX-ray2.40B2-108[»]
1SKSX-ray2.30B2-108[»]
1SKWX-ray2.30B2-108[»]
1SL0X-ray3.20B/D2-108[»]
1SL1X-ray2.20B2-108[»]
1SL2X-ray2.30B2-108[»]
1SRXX-ray2.80A2-109[»]
1T7PX-ray2.20B2-108[»]
1T8EX-ray2.54B2-108[»]
1THOX-ray2.30A2-108[»]
1TK0X-ray2.30B2-108[»]
1TK5X-ray2.20B2-108[»]
1TK8X-ray2.50B2-108[»]
1TKDX-ray2.49B2-108[»]
1TXXX-ray2.20A2-109[»]
1X9MX-ray2.10B2-108[»]
1X9SX-ray2.70B2-108[»]
1X9WX-ray2.30B2-108[»]
1XOANMR-A2-109[»]
1XOBNMR-A2-109[»]
1ZCPX-ray2.30A/B/C/D2-108[»]
1ZYQX-ray2.70B2-108[»]
1ZZYX-ray2.50A/B2-109[»]
2AJQX-ray2.60B/I2-108[»]
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/G2-108[»]
2FD3X-ray2.45A/B2-108[»]
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[»]
ProteinModelPortalP0AA25.
SMRP0AA25. Positions 2-109.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-31856N.
IntActP0AA25. 98 interactions.
MINTMINT-1530752.
STRING511145.b3781.

2D gel databases

SWISS-2DPAGEP0AA25.

Proteomic databases

PaxDbP0AA25.
PRIDEP0AA25.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76786; AAC76786; b3781.
BAE77517; BAE77517; BAE77517.
GeneID12934322.
948289.
KEGGecj:Y75_p3394.
eco:b3781.
PATRIC32123053. VBIEscCol129921_3896.

Organism-specific databases

EchoBASEEB1024.
EcoGeneEG11031. trxA.

Phylogenomic databases

eggNOGCOG0526.
HOGENOMHOG000292977.
KOK03671.
OMASDKIVYL.
OrthoDBEOG6QG8RK.
PhylomeDBP0AA25.
ProtClustDBPRK09381.

Enzyme and pathway databases

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

Gene expression databases

GenevestigatorP0AA25.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERPTHR10438. PTHR10438. 1 hit.
PfamPF00085. Thioredoxin. 1 hit.
[Graphical view]
PIRSFPIRSF000077. Thioredoxin. 1 hit.
PRINTSPR00421. THIOREDOXIN.
SUPFAMSSF52833. SSF52833. 1 hit.
TIGRFAMsTIGR01068. thioredoxin. 1 hit.
PROSITEPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0AA25.
PROP0AA25.

Entry information

Entry nameTHIO_ECOLI
AccessionPrimary (citable) accession number: P0AA25
Secondary accession number(s): P00274 expand/collapse secondary AC list , P76750, Q2M889, Q47674, Q8XAT2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

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