Identification
Name:Thioredoxin-1
Synonyms:
  • Trx-1
Gene Name:trxA
Enzyme Class:Not Available
Biological Properties
General Function:Involved in electron carrier activity
Specific Function:Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions
Cellular Location:Not Available
SMPDB Pathways:Not Available
KEGG Pathways:Not Available
Complex Reactions:
1.0Thumb+1.0Reduced Thioredoxin1.0Thumb+1.0Thumb+1.0Oxidized Thioredoxin
1.0ADP + 1.0Reduced Thioredoxin → 1.0dADP + 1.0Water + 1.0Oxidized Thioredoxin
ReactionCard
1.0Thumb+1.0Reduced Thioredoxin1.0Thumb+1.0Thumb+1.0Oxidized Thioredoxin
1.0Guanosine diphosphate + 1.0Reduced Thioredoxin → 1.0dGDP + 1.0Water + 1.0Oxidized Thioredoxin
ReactionCard
1.0Thumb+1.0Reduced Thioredoxin1.0Thumb+1.0Thumb+1.0Oxidized Thioredoxin
1.0CDP + 1.0Reduced Thioredoxin → 1.0dCDP + 1.0Water + 1.0Oxidized Thioredoxin
ReactionCard
1.0Reduced Thioredoxin+1.0Thumb1.0Thumb+1.0Thumb+1.0Oxidized Thioredoxin
1.0Reduced Thioredoxin + 1.0Uridine 5'-diphosphate → 1.0dUDP + 1.0Water + 1.0Oxidized Thioredoxin
ReactionCard
1.0Thumb+1.0Reduced Thioredoxin1.0Thumb+1.0Thumb+1.0Oxidized Thioredoxin
1.0Methionine sulfoxide + 1.0Reduced Thioredoxin → 1.0Water + 1.0L-Methionine + 1.0Oxidized Thioredoxin
ReactionCard
1.0Thumb+1.0Reduced Thioredoxin2.0Thumb+1.0Oxidized Thioredoxin
1.0Hydrogen peroxide + 1.0Reduced Thioredoxin → 2.0Water + 1.0Oxidized Thioredoxin
ReactionCard
1.0Thumb+1.0Reduced Thioredoxin2.0Thumb+1.0Thumb+1.0Thumb+1.0Oxidized Thioredoxin
1.0Phosphoadenosine phosphosulfate + 1.0Reduced Thioredoxin → 2.0Hydrogen ion + 1.0Adenosine 3',5'-diphosphate + 1.0Sulfite + 1.0Oxidized Thioredoxin
ReactionCard
1.0Thumb+1.0Thumb+1.0Oxidized Thioredoxin1.0Thumb+1.0Reduced Thioredoxin
1.0Hydrogen ion + 1.0NADPH + 1.0Oxidized Thioredoxin → 1.0NADP + 1.0Reduced Thioredoxin
ReactionCard
1.0fused thiol:disulfide interchange protein (oxidized)+1.0Reduced Thioredoxin1.0fused thiol:disulfide interchange protein (reduced)+1.0Oxidized Thioredoxin
1.0fused thiol:disulfide interchange protein (oxidized) + 1.0Reduced Thioredoxin → 1.0fused thiol:disulfide interchange protein (reduced) + 1.0Oxidized Thioredoxin
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00061Adenosine 3',5'-diphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB01546CDPMetaboCard
ECMDB21326dADPMetaboCard
ECMDB01245dCDPMetaboCard
ECMDB00960dGDPMetaboCard
ECMDB01000dUDPMetaboCard
ECMDB01201Guanosine diphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21232Hydrogen peroxideMetaboCard
ECMDB00696L-MethionineMetaboCard
ECMDB02005Methionine sulfoxideMetaboCard
ECMDB00217NADPMetaboCard
ECMDB04111NADPHMetaboCard
ECMDB01134Phosphoadenosine phosphosulfateMetaboCard
ECMDB21283SelenodiglutathioneMetaboCard
ECMDB00240SulfiteMetaboCard
ECMDB00295Uridine 5'-diphosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
catalytic activity
disulfide oxidoreductase activity
electron carrier activity
oxidoreductase activity
oxidoreductase activity, acting on a sulfur group of donors
protein disulfide oxidoreductase activity
Process
cell redox homeostasis
cellular homeostasis
cellular process
glycerol ether metabolic process
metabolic process
organic ether metabolic process
small molecule metabolic process
Gene Properties
Blattner:b3781
Gene OrientationClockwise
Centisome Percentage:85.43
Left Sequence End3963784
Right Sequence End3964113
Gene Sequence:
>330 bp
ATGTTTGGTAAAGGCGGTCTGGGTAACCTGATGAAGCAAGCCCAGCAGATGCAAGAAAAA
ATGCAGAAAATGCAGGAAGAGATCGCGCAGCTGGAAGTCACCGGCGAATCTGGCGCAGGT
CTGGTAAAAGTGACCATCAACGGTGCACACAACTGCCGTCGCGTAGAGATCGACCCGAGC
CTGCTGGAAGACGACAAAGAGATGCTGGAAGACCTGGTGGCTGCAGCATTCAACGACGCA
GCACGTCGTATTGAAGAAACGCAGAAAGAAAAAATGGCCTCTGTATCCTCCGGAATGCAG
CTGCCGCCTGGCTTTAAGATGCCGTTCTGA
Protein Properties
Pfam Domain Function:
Protein Residues:109
Protein Molecular Weight:11807
Protein Theoretical pI:4
PDB File:1SL2
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Thioredoxin-1
MSDKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEYQGKLTVAKLN
IDQNPGTAPKYGIRGIPTLLLFKNGEVAATKVGALSKGQLKEFLDANLA
References
External Links:
ResourceLink
Uniprot ID:P0AA25
Uniprot Name:THIO_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674610
PDB ID:1SL2
Ecogene ID:EG11031
Ecocyc:EG11031
ColiBase:b3781
Kegg Gene:b3781
EchoBASE ID:EB1024
CCDB:THIO_ECOLI
BacMap:67005950
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, 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. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Daniels, D. L., Plunkett, G. 3rd, Burland, V., Blattner, F. R. (1992). "Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes." Science 257:771-778. Pubmed: 1379743
  • Dyson, H. J., Gippert, G. P., Case, D. A., Holmgren, A., Wright, P. E. (1990). "Three-dimensional solution structure of the reduced form of Escherichia coli thioredoxin determined by nuclear magnetic resonance spectroscopy." Biochemistry 29:4129-4136. Pubmed: 2193685
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Holmgren, A. (1968). "Thioredoxin. 6. The amino acid sequence of the protein from escherichia coli B." Eur J Biochem 6:475-484. Pubmed: 4883076
  • Holmgren, A., Soderberg, B. O., Eklund, H., Branden, C. I. (1975). "Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution." Proc Natl Acad Sci U S A 72:2305-2309. Pubmed: 1094461
  • Hoog, J. O., von Bahr-Lindstrom, H., Josephson, S., Wallace, B. J., Kushner, S. R., Jornvall, H., Holmgren, A. (1984). "Nucleotide sequence of the thioredoxin gene from Escherichia coli." Biosci Rep 4:917-923. Pubmed: 6098320
  • Jeng, M. F., Campbell, A. P., Begley, T., Holmgren, A., Case, D. A., Wright, P. E., Dyson, H. J. (1994). "High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin." Structure 2:853-868. Pubmed: 7812718
  • Katti, S. K., LeMaster, D. M., Eklund, H. (1990). "Crystal structure of thioredoxin from Escherichia coli at 1.68 A resolution." J Mol Biol 212:167-184. Pubmed: 2181145
  • Lennon, B. W., Williams, C. H. Jr, Ludwig, M. L. (2000). "Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductase." Science 289:1190-1194. Pubmed: 10947986
  • Lim, C. J., Geraghty, D., Fuchs, J. A. (1985). "Cloning and nucleotide sequence of the trxA gene of Escherichia coli K-12." J Bacteriol 163:311-316. Pubmed: 3891733
  • Nikkola, M., Gleason, F. K., Fuchs, J. A., Eklund, H. (1993). "Crystal structure analysis of a mutant Escherichia coli thioredoxin in which lysine 36 is replaced by glutamic acid." Biochemistry 32:5093-5098. Pubmed: 8098620
  • Schultz, L. W., Chivers, P. T., Raines, R. T. (1999). "The CXXC motif: crystal structure of an active-site variant of Escherichia coli thioredoxin." Acta Crystallogr D Biol Crystallogr 55:1533-1538. Pubmed: 10489448
  • Soderberg, B. O., Holmgren, A., Branden, C. I. (1974). "Structure of oxidized thioredoxin to 4 with 5 A resolution." J Mol Biol 90:143-152. Pubmed: 4616096
  • Wallace, B. J., Kushner, S. R. (1984). "Genetic and physical analysis of the thioredoxin (trxA) gene of Escherichia coli K-12." Gene 32:399-408. Pubmed: 6099324
  • Zhang, J., Sprung, R., Pei, J., Tan, X., Kim, S., Zhu, H., Liu, C. F., Grishin, N. V., Zhao, Y. (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8:215-225. Pubmed: 18723842