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  • Thioredoxin II
  • TR-II
  • Thioredoxin-1
Gene NameTRX2
Enzyme ClassNot Available
Biological Properties
General FunctionInvolved in electron carrier activity
Specific FunctionParticipates as a hydrogen donor in redox reactions through the reversible oxidation of its active center dithiol to a disulfide, accompanied by the transfer of 2 electrons and 2 protons. It is involved in many cellular processes, including deoxyribonucleotide synthesis, repair of oxidatively damaged proteins, protein folding, sulfur metabolism, and redox homeostasis. Thioredoxin-dependent enzymes include phosphoadenosine-phosphosulfate reductase MET16, alkyl- hydroperoxide reductase DOT5, thioredoxin peroxidases TSA1 and TSA2, alkyl hydroperoxide reductase AHP1, and peroxiredoxin HYR1. Thioredoxin is also involved in protection against reducing stress. As part of the LMA1 complex, it is involved in the facilitation of vesicle fusion such as homotypic vacuole and ER- derived COPII vesicle fusion with the Golgi. This activity does not require the redox mechanism. Through its capacity to inactivate the stress response transcription factor YAP1 and its regulator the hydroperoxide stress sensor HYR1, it is involved in feedback regulation of stress response gene expression upon oxidative stress
Cellular LocationCytoplasm. Golgi apparatus membrane; Peripheral membrane protein. Nucleus
SMPDB PathwaysNot Available
KEGG PathwaysNot Available
SMPDB ReactionsNot Available
KEGG Reactions
Adenosine triphosphate + thioredoxin dithiol → dATP + thioredoxin disulfide + water
thioredoxin dithiol + Cytidine triphosphate → thioredoxin disulfide + water + dCTP
GTP + thioredoxin dithiol → thioredoxin disulfide + water + dGTP
Uridine triphosphate + thioredoxin dithiol → thioredoxin disulfide + Deoxyuridine triphosphate + water
YMDB00109Adenosine triphosphateShow
YMDB00201Deoxyuridine triphosphateShow
YMDB00279Cytidine triphosphateShow
YMDB00326Uridine triphosphateShow
YMDB00888Hydrogen peroxideShow
GO Classification
Not Available
electron carrier activity
oxidoreductase activity, acting on a sulfur group of donors
disulfide oxidoreductase activity
protein disulfide oxidoreductase activity
catalytic activity
oxidoreductase activity
small molecule metabolic process
cellular process
cellular homeostasis
cell redox homeostasis
organic ether metabolic process
glycerol ether metabolic process
metabolic process
Gene Properties
Chromosome Locationchromosome 7
Protein Properties
Pfam Domain Function
Protein Residues104
Protein Molecular Weight11203.7998
Protein Theoretical pI4.54
Signalling Regions
  • None
Transmembrane Regions
  • None
External Links
Saccharomyces Genome Database TRX2
Uniprot IDP22803
Uniprot NameTRX2_YEAST
GenBank Gene IDAY557817
Genebank Protein ID45269525
General Reference
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  • Hall, D. E., Baldesten, A., Holmgren, A., Reichard, P. (1971). "Yeast thioredoxin. Amino-acid sequence around the active-center disulfide of thioredoxin I and II." Eur J Biochem 23:328-335.4945270
  • Schwenn, J. D., Krone, F. A., Husmann, K. (1988). "Yeast PAPS reductase: properties and requirements of the purified enzyme." Arch Microbiol 150:313-319.3060034
  • Xu, Z., Mayer, A., Muller, E., Wickner, W. (1997). "A heterodimer of thioredoxin and I(B)2 cooperates with Sec18p (NSF) to promote yeast vacuole inheritance." J Cell Biol 136:299-306.9015301
  • Xu, Z., Sato, K., Wickner, W. (1998). "LMA1 binds to vacuoles at Sec18p (NSF), transfers upon ATP hydrolysis to a t-SNARE (Vam3p) complex, and is released during fusion." Cell 93:1125-1134.9657146
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  • Lee, J., Spector, D., Godon, C., Labarre, J., Toledano, M. B. (1999). "A new antioxidant with alkyl hydroperoxide defense properties in yeast." J Biol Chem 274:4537-4544.9988687
  • Delaunay, A., Isnard, A. D., Toledano, M. B. (2000). "H2O2 sensing through oxidation of the Yap1 transcription factor." EMBO J 19:5157-5166.11013218
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  • Trotter, E. W., Grant, C. M. (2002). "Thioredoxins are required for protection against a reductive stress in the yeast Saccharomyces cerevisiae." Mol Microbiol 46:869-878.12410842
  • Carmel-Harel, O., Storz, G. (2000). "Roles of the glutathione- and thioredoxin-dependent reduction systems in the Escherichia coli and saccharomyces cerevisiae responses to oxidative stress." Annu Rev Microbiol 54:439-461.11018134
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  • Elazar, Z., Scherz-Shouval, R., Shorer, H. (2003). "Involvement of LMA1 and GATE-16 family members in intracellular membrane dynamics." Biochim Biophys Acta 1641:145-156.12914955
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  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V., Eng, J., Zhou, H. (2008). "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Mol Cell Proteomics 7:1389-1396.18407956
  • Bao, R., Chen, Y., Tang, Y. J., Janin, J., Zhou, C. Z. (2007). "Crystal structure of the yeast cytoplasmic thioredoxin Trx2." Proteins 66:246-249.17044062