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folD protein (Pedobacter sp. BAL39) - STRING interaction network
"folD" - Bifunctional protein FolD in Pedobacter sp. BAL39
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second shell of interactors
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some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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folDBifunctional protein FolD ; Catalyzes the oxidation of 5,10- methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10- formyltetrahydrofolate (293 aa)    
Predicted Functional Partners:
glyA
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 (423 aa)
 
  0.972
purN
GAR transformylase ; Catalyzes the transfer of a formyl group from 10- formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate (228 aa)
 
 
  0.967
gcvP
Glycine dehydrogenase (aminomethyl-transferring) ; 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 (959 aa)
   
 
  0.963
PBAL39_07145
Bifunctional purine biosynthesis protein PurH (508 aa)
 
 
  0.962
gcvT
Glycine cleavage system T protein ; The glycine cleavage system catalyzes the degradation of glycine (359 aa)
   
 
  0.948
fmt
Methionyl-tRNA formyltransferase ; Modifies the free amino group of the aminoacyl moiety of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by- (I) promoting its recognition by IF2 and (II) impairing its binding to EFTu-GTP (297 aa)
 
 
  0.948
PBAL39_04663
Methylenetetrahydrofolate reductase (318 aa)
   
 
  0.930
PBAL39_09801
Phosphoribosylamine--glycine ligase (Phosphoribosylglycinamide synthetase) (GARS) (405 aa)
   
 
  0.926
PBAL39_06231
Folylpolyglutamate synthase (412 aa)
 
  0.920
PBAL39_04658
Methionine synthase (1219 aa)
   
 
  0.911
Your Current Organism:
Pedobacter sp. BAL39
NCBI taxonomy Id: 391596
Other names: P. sp. BAL39, Pedobacter BAL39, Pedobacter sp. BAL39
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