Glutaredoxin-2, mitochondrial (P17695)

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 + Glutathione ↔ water + Oxidized glutathione
Metabolites
YMDB IDNameView
YMDB00057Oxidized glutathioneShow
YMDB00160GlutathioneShow
YMDB00426NADPHShow
YMDB00427NADPShow
YMDB00693glutathione disulfideShow
YMDB00862hydronShow
YMDB00888Hydrogen peroxideShow
YMDB00890waterShow
GO Classification
Component
Not Available
Function
catalytic activity
oxidoreductase activity
electron carrier activity
oxidoreductase activity, acting on a sulfur group of donors
disulfide oxidoreductase activity
protein disulfide oxidoreductase 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