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GRX8 protein (Saccharomyces cerevisiae) - STRING interaction network
"GRX8" - Glutaredoxin that employs a dithiol mechanism of catalysis in Saccharomyces cerevisiae
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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GRX8Glutaredoxin that employs a dithiol mechanism of catalysis; monomeric; activity is low and null mutation does not affect sensitivity to oxidative stress; GFP-fusion protein localizes to the cytoplasm; expression strongly induced by arsenic; Glutathione-dependent oxidoreductase with lower activity compared to the other members of the glutaredoxin family. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase (109 aa)    
Predicted Functional Partners:
TRR2
Mitochondrial thioredoxin reductase involved in protection against oxidative stress, required with Glr1p to maintain the redox state of Trx3p; contains active-site motif (CAVC) present in prokaryotic orthologs; binds NADPH and FAD; Acts on mitochondrial thioredoxin 3. Implicated in the defense against oxidative stress (342 aa)
   
 
  0.856
TRR1
Cytoplasmic thioredoxin reductase, key regulatory enzyme that determines the redox state of the thioredoxin system, which acts as a disulfide reductase system and protects cells against both oxidative and reductive stress; Acts on thioredoxins 1 and 2 (319 aa)
   
 
  0.793
GRX3
Hydroperoxide and superoxide-radical responsive glutathione-dependent oxidoreductase; monothiol glutaredoxin subfamily member along with Grx4p and Grx5p; protects cells from oxidative damage; Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters (By similarity). Binds one iron-sulfur cluster per dimer. The iron-sulfur cluster is bound between subunits, and is complexed by a bound glutathione and a cysteine residue from each subunit (Probable) (285 aa)
   
 
  0.759
GRX5
Hydroperoxide and superoxide-radical responsive glutathione-dependent oxidoreductase; mitochondrial matrix protein involved in the synthesis/assembly of iron-sulfur centers; monothiol glutaredoxin subfamily member along with Grx3p and Grx4p; Monothiol glutaredoxin involved in iron-sulfur biogenesis. Required for normal iron homeostasis. Protects cells against oxidative damage due to reactive oxygen species (150 aa)
   
 
  0.688
TRX3
Mitochondrial thioredoxin, highly conserved oxidoreductase required to maintain the redox homeostasis of the cell, forms the mitochondrial thioredoxin system with Trr2p, redox state is maintained by both Trr2p and Glr1p (127 aa)
   
   
  0.677
GRX7
Cis-golgi localized monothiol glutaredoxin; more similar in activity to dithiol than other monothiol glutaredoxins; involved in the oxidative stress response; does not bind metal ions; functional overlap with GRX6 (203 aa)
           
  0.642
HAM1
Conserved protein with deoxyribonucleoside triphosphate pyrophosphohydrolase activity, mediates exclusion of noncanonical purines from deoxyribonucleoside triphosphate pools; mutant is sensitive to the base analog 6-N-hydroxylaminopurine; Pyrophosphatase that hydrolyzes the non-canonical purine nucleotides inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) as well as 2’-deoxy-N-6-hydroxylaminopurine triposphate (dHAPTP) and 5-bromodeoxyuridine 5’-triphosphate (BrdUTP) to their respective monophosphate derivatives. Xanthosine 5’-triphosphate (XTP) is also a potential substrate [...] (197 aa)
     
 
    0.624
YNK1
Nucleoside diphosphate kinase, catalyzes the transfer of gamma phosphates from nucleoside triphosphates, usually ATP, to nucleoside diphosphates by a mechanism that involves formation of an autophosphorylated enzyme intermediate; Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Required for repair of UV radiation- and etoposide-induced DNA damage (153 aa)
     
 
  0.622
ADK2
Mitochondrial adenylate kinase, catalyzes the reversible synthesis of GTP and AMP from GDP and ADP; may serve as a back-up for synthesizing GTP or ADP depending on metabolic conditions; 3’ sequence of ADK2 varies with strain background; Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways (225 aa)
     
 
    0.613
ADK1
Adenylate kinase, required for purine metabolism; localized to the cytoplasm and the mitochondria; lacks cleavable signal sequence; Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways (222 aa)
     
 
    0.613
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: Candida robusta, Pachytichospora, S. cerevisiae, Saccharomyces, Saccharomyces capensis, Saccharomyces cerevisiae, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
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