| Identification |
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| Name | Glutaredoxin-1 |
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| Synonyms | - Glutathione-dependent oxidoreductase 1
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| Gene Name | GRX1 |
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| Enzyme Class | Not Available |
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| Biological Properties |
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| General Function | Involved in electron carrier activity |
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| Specific Function | Multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S- transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage |
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| Cellular Location | Cytoplasm |
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| SMPDB Pathways | Not Available |
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| KEGG Pathways | Not Available |
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| SMPDB Reactions | Not Available |
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| KEGG Reactions | |
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| Metabolites | | YMDB ID | Name | View |
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| YMDB00057 | Oxidized glutathione | Show | | YMDB00160 | Glutathione | Show | | YMDB00426 | NADPH | Show | | YMDB00427 | NADP | Show | | YMDB00693 | glutathione disulfide | Show | | YMDB00862 | hydron | Show | | YMDB00888 | Hydrogen peroxide | Show | | YMDB00890 | water | Show |
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| GO Classification | | Component |
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| Not Available | | Function |
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| catalytic activity | | oxidoreductase activity | | electron carrier activity | | oxidoreductase activity, acting on a sulfur group of donors | | disulfide oxidoreductase activity | | protein disulfide oxidoreductase activity | | Process |
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| cellular process | | cellular homeostasis | | cell redox homeostasis |
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| Gene Properties |
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| Chromosome Location | chromosome 3 |
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| Locus | YCL035C |
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| Gene Sequence | >333 bp
ATGGTATCTCAAGAAACTATCAAGCACGTCAAGGACCTTATTGCAGAAAACGAGATCTTC
GTCGCATCCAAAACGTACTGTCCATACTGCCATGCAGCCCTAAACACGCTTTTTGAAAAG
TTAAAGGTTCCCAGGTCCAAAGTTCTGGTTTTGCAATTGAATGACATGAAGGAAGGCGCA
GACATTCAGGCTGCGTTATATGAGATTAATGGCCAAAGAACCGTGCCAAACATCTATATT
AATGGTAAACATATTGGAGGCAACGACGACTTGCAGGAATTGAGGGAGACTGGTGAATTG
GAGGAATTGTTAGAACCTATTCTTGCAAATTAA |
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| Protein Properties |
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| Pfam Domain Function | |
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| Protein Residues | 110 |
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| Protein Molecular Weight | 12380.09961 |
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| Protein Theoretical pI | 4.72 |
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| Signalling Regions | |
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| Transmembrane Regions | |
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| Protein Sequence | >Glutaredoxin-1
MVSQETIKHVKDLIAENEIFVASKTYCPYCHAALNTLFEKLKVPRSKVLVLQLNDMKEGA
DIQAALYEINGQRTVPNIYINGKHIGGNDDLQELRETGELEELLEPILAN |
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| References |
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| External Links | |
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| General Reference | - Oliver, S. G., van der Aart, Q. J., Agostoni-Carbone, M. L., Aigle, M., Alberghina, L., Alexandraki, D., Antoine, G., Anwar, R., Ballesta, J. P., Benit, P., et, a. l. .. (1992). "The complete DNA sequence of yeast chromosome III." Nature 357:38-46.1574125
- Luikenhuis, S., Perrone, G., Dawes, I. W., Grant, C. M. (1998). "The yeast Saccharomyces cerevisiae contains two glutaredoxin genes that are required for protection against reactive oxygen species." Mol Biol Cell 9:1081-1091.9571241
- Grant, C. M., Luikenhuis, S., Beckhouse, A., Soderbergh, M., Dawes, I. W. (2000). "Differential regulation of glutaredoxin gene expression in response to stress conditions in the yeast Saccharomyces cerevisiae." Biochim Biophys Acta 1490:33-42.10786615
- Collinson, E. J., Wheeler, G. L., Garrido, E. O., Avery, A. M., Avery, S. V., Grant, C. M. (2002). "The yeast glutaredoxins are active as glutathione peroxidases." J Biol Chem 277:16712-16717.11875065
- Collinson, E. J., Grant, C. M. (2003). "Role of yeast glutaredoxins as glutathione S-transferases." J Biol Chem 278:22492-22497.12684511
- 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
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