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gcvH protein (Idiomarina loihiensis) - STRING interaction network
"gcvH" - Glycine cleavage system protein H in Idiomarina loihiensis
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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gcvHGlycine cleavage system protein H; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein (129 aa)    
Predicted Functional Partners:
gcvT
Glycine cleavage system T protein; The glycine cleavage system catalyzes the degradation of glycine (359 aa)
 
  0.999
gcvP
Glycine dehydrogenase; The glycine cleavage system 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 (962 aa)
 
  0.999
glyA
Glycine/serine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF- independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism (418 aa)
   
 
  0.993
lpd
Dihydrolipoamide dehydrogenase (475 aa)
 
 
  0.976
lplA
Lipoate-protein ligase A (349 aa)
 
  0.932
gltB
Glutamate synthase subunit alpha (1488 aa)
     
 
  0.898
lipA
Lipoyl 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 (310 aa)
 
 
  0.853
IL1646
Mercuric reductase (467 aa)
 
 
  0.851
IL1160
Mercuric reductase (730 aa)
   
 
  0.835
lipB
Lipoate-protein ligase B; 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 (221 aa)
   
  0.829
Your Current Organism:
Idiomarina loihiensis
NCBI taxonomy Id: 283942
Other names: I. loihiensis, I. loihiensis L2TR, Idiomarina loihiensis, Idiomarina loihiensis Donachie et al. 2003, Idiomarina loihiensis L2TR, Idiomarina loihiensis str. L2TR, Idiomarina loihiensis strain L2TR
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