STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
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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[Homology]
Score
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
Glycine 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.
  
 0.976
purH
Bifunctional purine biosynthesis protein purH; KEGG: pmf:P9303_24851 bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; PFAM: AICARFT/IMPCHase bienzyme, transformylase domain; Methylglyoxal synthase-like domain; TIGRFAM: AICARFT/IMPCHase bienzyme; HAMAP: AICARFT/IMPCHase bienzyme; SMART: AICARFT/IMPCHase bienzyme, transformylase domain; Methylglyoxal synthase-like domain.
 
 
 0.966
gcvP
Glycine dehydrogenase (decarboxylating); 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; Belongs to the GcvP family.
  
 
 0.964
EHA63389.1
Methionine synthase; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate.
    
 0.956
fmt
Methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family.
 
 
 0.955
purN
Phosphoribosylglycinamide formyltransferase; 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.
 
 
 0.955
gcvT
Aminomethyltransferase; The glycine cleavage system catalyzes the degradation of glycine.
  
 
 0.947
purU
Formyltetrahydrofolate deformylase; Catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to formate and tetrahydrofolate (FH4).
 
 
 0.936
EHA60101.1
FolC bifunctional protein; KEGG: pmt:PMT0330 putative bifunctional dihydrofolate/folylpolyglutamate synthase; TIGRFAM: Folylpolyglutamate synthetase; PFAM: Mur ligase, C-terminal.
 
  
 0.935
EHA63059.1
KEGG: pmf:P9303_08921 5-formyltetrahydrofolate cyclo-ligase; TIGRFAM: 5-formyltetrahydrofolate cyclo-ligase; PFAM: 5-formyltetrahydrofolate cyclo-ligase; Belongs to the 5-formyltetrahydrofolate cyclo-ligase family.
    
 0.916
Your Current Organism:
Synechococcus sp. WH 8016
NCBI taxonomy Id: 166318
Other names: S. sp. WH 8016, Synechococcus sp. WH8016
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