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Identification
NameGlutaredoxin-2, mitochondrial
Synonyms
  • Glutathione-dependent oxidoreductase 2
  • Thioltransferase
Gene NameGRX2
Enzyme ClassNot Available
Biological Properties
General FunctionInvolved in electron carrier activity
Specific FunctionMultifunctional 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
Cellular LocationCytoplasm. Mitochondrion.
SMPDB PathwaysNot Available
KEGG PathwaysNot Available
SMPDB ReactionsNot Available
KEGG Reactions
Hydrogen peroxide + Glutathionewater + Oxidized glutathione
Metabolites
YMDB IDNameView
YMDB00057Oxidized glutathioneShow
YMDB00160GlutathioneShow
YMDB00426NADPHShow
YMDB00427NADPShow
YMDB00693glutathione disulfideShow
YMDB00862hydronShow
YMDB00888Hydrogen peroxideShow
YMDB00890waterShow
GO Classification
Component
Not Available
Function
oxidoreductase activity, acting on a sulfur group of donors
disulfide oxidoreductase activity
protein disulfide oxidoreductase activity
catalytic activity
oxidoreductase activity
electron carrier activity
Process
cellular process
cellular homeostasis
cell redox homeostasis
Gene Properties
Chromosome Locationchromosome 4
LocusYDR513W
Gene Sequence>432 bp ATGGAGACCAATTTTTCCTTCGACTCGAATTTAATTGTTATTATCATTATCACGTTGTTT GCCACAAGAATTATTGCTAAAAGATTTTTATCTACTCCAAAAATGGTATCCCAGGAAACA GTTGCTCACGTAAAGGATCTGATTGGCCAAAAGGAAGTGTTTGTTGCAGCAAAGACATAC TGCCCTTACTGTAAAGCTACTTTGTCTACCCTCTTCCAAGAATTGAACGTTCCCAAATCC AAGGCCCTTGTGTTGGAATTAGATGAAATGAGCAATGGCTCAGAGATTCAAGACGCTTTA GAAGAAATCTCGGGCCAAAAAACTGTACCTAACGTATACATCAATGGCAAGCACATTGGT GGTAACAGCGATTTGGAAACTTTGAAGAAAAATGGCAAGTTAGCTGAAATATTGAAGCCG GTATTTCAATAG
Protein Properties
Pfam Domain Function
Protein Residues143
Protein Molecular Weight15861.2998
Protein Theoretical pI7.41
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Glutaredoxin-2, mitochondrial METNFSFDSNLIVIIIITLFATRIIAKRFLSTPKMVSQETVAHVKDLIGQKEVFVAAKTY CPYCKATLSTLFQELNVPKSKALVLELDEMSNGSEIQDALEEISGQKTVPNVYINGKHIG GNSDLETLKKNGKLAEILKPVFQ
References
External Links
ResourceLink
Saccharomyces Genome Database GRX2
Uniprot IDP17695
Uniprot NameGLRX2_YEAST
GenBank Gene IDAY692896
Genebank Protein ID51013243
General Reference
  • Gan, Z. R. (1992). "Cloning and sequencing of a gene encoding yeast thioltransferase." Biochem Biophys Res Commun 187:949-955.1530649
  • Jacq, C., Alt-Morbe, J., Andre, B., Arnold, W., Bahr, A., Ballesta, J. P., Bargues, M., Baron, L., Becker, A., Biteau, N., Blocker, H., Blugeon, C., Boskovic, J., Brandt, P., Bruckner, M., Buitrago, M. J., Coster, F., Delaveau, T., del Rey, F., Dujon, B., Eide, L. G., Garcia-Cantalejo, J. M., Goffeau, A., Gomez-Peris, A., Zaccaria, P., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Nature 387:75-78.9169867
  • 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
  • Gan, Z. R., Polokoff, M. A., Jacobs, J. W., Sardana, M. K. (1990). "Complete amino acid sequence of yeast thioltransferase (glutaredoxin)." Biochem Biophys Res Commun 168:944-951.2189409
  • 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
  • Pedrajas, J. R., Porras, P., Martinez-Galisteo, E., Padilla, C. A., Miranda-Vizuete, A., Barcena, J. A. (2002). "Two isoforms of Saccharomyces cerevisiae glutaredoxin 2 are expressed in vivo and localize to different subcellular compartments." Biochem J 364:617-623.11958675
  • 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
  • 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