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Identification
NameThioredoxin-1
Synonyms
  • Thioredoxin I
  • TR-I
  • Thioredoxin-2
Gene NameTRX1
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
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
Metabolites
YMDB IDNameView
YMDB00109Adenosine triphosphateShow
YMDB00201Deoxyuridine triphosphateShow
YMDB00279Cytidine triphosphateShow
YMDB00326Uridine triphosphateShow
YMDB00426NADPHShow
YMDB00427NADPShow
YMDB00558GTPShow
YMDB00658dCTPShow
YMDB00700dATPShow
YMDB00744dGTPShow
YMDB00862hydronShow
YMDB00888Hydrogen peroxideShow
YMDB00890waterShow
GO Classification
Component
Not Available
Function
oxidoreductase activity
electron carrier activity
oxidoreductase activity, acting on a sulfur group of donors
disulfide oxidoreductase activity
catalytic activity
protein disulfide oxidoreductase activity
Process
metabolic process
organic ether metabolic process
glycerol ether metabolic process
small molecule metabolic process
cellular process
cellular homeostasis
cell redox homeostasis
Gene Properties
Chromosome Locationchromosome 12
LocusYLR043C
Gene Sequence>312 bp ATGGTTACTCAATTCAAAACTGCCAGCGAATTCGACTCTGCAATTGCTCAAGACAAGCTA GTTGTCGTAGATTTCTACGCCACTTGGTGCGGTCCATGTAAAATGATTGCTCCAATGATT GAAAAATTCTCTGAACAATACCCACAAGCTGATTTCTATAAATTGGATGTCGATGAATTG GGTGATGTTGCACAAAAGAATGAAGTTTCCGCTATGCCAACTTTGCTTCTATTCAAGAAC GGTAAGGAAGTTGCAAAGGTTGTTGGTGCCAACCCAGCGGCTATTAAGCAAGCCATTGCT GCTAATGCTTAA
Protein Properties
Pfam Domain Function
Protein Residues103
Protein Molecular Weight11234.90039
Protein Theoretical pI4.54
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Thioredoxin-1 MVTQFKTASEFDSAIAQDKLVVVDFYATWCGPCKMIAPMIEKFSEQYPQADFYKLDVDEL GDVAQKNEVSAMPTLLLFKNGKEVAKVVGANPAAIKQAIAANA
References
External Links
ResourceLink
Saccharomyces Genome Database TRX1
Uniprot IDP22217
Uniprot NameTRX1_YEAST
GenBank Gene IDAY558203
Genebank Protein ID45270296
General Reference
  • Gan, Z. R. (1991). "Yeast thioredoxin genes." J Biol Chem 266:1692-1696.1988444
  • Muller, E. G. (1991). "Thioredoxin deficiency in yeast prolongs S phase and shortens the G1 interval of the cell cycle." J Biol Chem 266:9194-9202.2026619
  • Muller, E. G. (1992). "Thioredoxin genes in Saccharomyces cerevisiae: map positions of TRX1 and TRX2." Yeast 8:117-120.1561834
  • Johnston, M., Hillier, L., Riles, L., Albermann, K., Andre, B., Ansorge, W., Benes, V., Bruckner, M., Delius, H., Dubois, E., Dusterhoft, A., Entian, K. D., Floeth, M., Goffeau, A., Hebling, U., Heumann, K., Heuss-Neitzel, D., Hilbert, H., Hilger, F., Kleine, K., Kotter, P., Louis, E. J., Messenguy, F., Mewes, H. W., Hoheisel, J. D., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Nature 387:87-90.9169871
  • Hu, Y., Rolfs, A., Bhullar, B., Murthy, T. V., Zhu, C., Berger, M. F., Camargo, A. A., Kelley, F., McCarron, S., Jepson, D., Richardson, A., Raphael, J., Moreira, D., Taycher, E., Zuo, D., Mohr, S., Kane, M. F., Williamson, J., Simpson, A., Bulyk, M. L., Harlow, E., Marsischky, G., Kolodner, R. D., LaBaer, J. (2007). "Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Genome Res 17:536-543.17322287
  • Chae, H. Z., Chung, S. J., Rhee, S. G. (1994). "Thioredoxin-dependent peroxide reductase from yeast." J Biol Chem 269:27670-27678.7961686
  • 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
  • Park, S. G., Cha, M. K., Jeong, W., Kim, I. H. (2000). "Distinct physiological functions of thiol peroxidase isoenzymes in Saccharomyces cerevisiae." J Biol Chem 275:5723-5732.10681558
  • 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
  • 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
  • Delaunay, A., Pflieger, D., Barrault, M. B., Vinh, J., Toledano, M. B. (2002). "A thiol peroxidase is an H2O2 receptor and redox-transducer in gene activation." Cell 111:471-481.12437921
  • 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
  • Grant, C. M. (2001). "Role of the glutathione/glutaredoxin and thioredoxin systems in yeast growth and response to stress conditions." Mol Microbiol 39:533-541.11169096
  • 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
  • Huh, W. K., Falvo, J. V., Gerke, L. C., Carroll, A. S., Howson, R. W., Weissman, J. S., O'Shea, E. K. (2003). "Global analysis of protein localization in budding yeast." Nature 425:686-691.14562095
  • 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