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GCV3 protein (Saccharomyces cerevisiae) - STRING interaction network
"GCV3" - H subunit of the mitochondrial glycine decarboxylase complex, required for the catabolism of glycine to 5,10-methylene-THF in Saccharomyces cerevisiae
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Predicted Interactions
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GCV3H subunit of the mitochondrial glycine decarboxylase complex, required for the catabolism of glycine to 5,10-methylene-THF; also required for all protein lipoylation; expression is regulated by levels of 5,10-methylene-THF; The glycine cleavage system (glycine decarboxylase complex) catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein (By similarity) (170 aa)    
Predicted Functional Partners:
GCV1
T subunit of the mitochondrial glycine decarboxylase complex, required for the catabolism of glycine to 5,10-methylene-THF; expression is regulated by levels of levels of 5,10-methylene-THF in the cytoplasm; The glycine cleavage system (glycine decarboxylase complex) catalyzes the degradation of glycine (400 aa)
 
  0.999
GCV2
P subunit of the mitochondrial glycine decarboxylase complex, required for the catabolism of glycine to 5,10-methylene-THF; expression is regulated by levels of 5,10-methylene-THF in the cytoplasm; The glycine cleavage system (glycine decarboxylase complex) catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein (1034 aa)
   
  0.999
SHM2
Cytosolic serine hydroxymethyltransferase, converts serine to glycine plus 5,10 methylenetetrahydrofolate; major isoform involved in generating precursors for purine, pyrimidine, amino acid, and lipid biosynthesis; Interconversion of serine and glycine (469 aa)
   
 
  0.997
AIM22
Putative lipoate-protein ligase, required along with Lip2 and Lip5 for lipoylation of Lat1p and Kgd2p; similar to E. coli LplA; null mutant displays reduced frequency of mitochondrial genome loss; Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes (409 aa)
     
  0.993
LPD1
Dihydrolipoamide dehydrogenase, the lipoamide dehydrogenase component (E3) of the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase multi-enzyme complexes; Lipoamide dehydrogenase is a component of the alpha- ketoacid dehydrogenase complexes. This includes the pyruvate dehydrogenase complex, which catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). Acts also as component of the glycine cleavage system (glycine decarboxylase complex), which catalyzes the degradation of glycine (499 aa)
   
 
  0.990
MTD1
NAD-dependent 5,10-methylenetetrahydrafolate dehydrogenase, plays a catalytic role in oxidation of cytoplasmic one-carbon units; expression is regulated by Bas1p and Bas2p, repressed by adenine, and may be induced by inositol and choline; Catalyzes oxidation of cytoplasmic one-carbon units for purine biosynthesis (320 aa)
   
 
  0.987
SHM1
Mitochondrial serine hydroxymethyltransferase, converts serine to glycine plus 5,10 methylenetetrahydrofolate; involved in generating precursors for purine, pyrimidine, amino acid, and lipid biosynthesis; reverse reaction generates serine; Interconversion of serine and glycine (490 aa)
   
 
  0.984
LIP5
Protein involved in biosynthesis of the coenzyme lipoic acid, has similarity to E. coli lipoic acid synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives (414 aa)
   
 
  0.972
LIP2
Lipoyl ligase, involved in the modification of mitochondrial enzymes by the attachment of lipoic acid groups; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate (By similarity) (328 aa)
   
  0.969
IRC15
Microtubule associated protein; regulates microtubule dynamics; required for accurate meiotic chromosome segregation; null mutant displays large budded cells due to delayed mitotic progression, increased levels of spontaneous Rad52 foci (499 aa)
   
 
  0.964
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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