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
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
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Textmining
[Homology]
Score
glyASerine 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. (413 aa)    
Predicted Functional Partners:
gcvT
Glycine cleavage system protein T; The glycine cleavage system catalyzes the degradation of glycine.
 
 0.997
purH
Phosphoribosylaminoimidazolecarboxamide formyltransferase; Involved in de novo purine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.985
upp
Uracil phosphoribosyltransferase; Catalyzes the conversion of uracil and 5-phospho-alpha-D- ribose 1-diphosphate (PRPP) to UMP and diphosphate.
  
  
 0.961
folD
Methenyltetrahydrofolate cyclohydrolase; Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- methenyltetrahydrofolate to 10-formyltetrahydrofolate.
  
 0.959
gcvPB
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; Belongs to the GcvP family. C-terminal subunit subfamily.
  
 
 0.958
fhs
Formate--tetrahydrofolate ligase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the formate--tetrahydrofolate ligase family.
  
 0.957
metH
Homocysteine methyltransferase; Catalyzes the formation of 5,10-methylenetetrahydrofolate from 5-methyltetrahydrofolate and S-adenosyl-L-homocysteine and methionine from S-adenosyl-L-methionine and L-homocysteine; expressed in B. subtilis under methionine starvation conditions; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.953
gcvH
Glycine cleavage system protein H; Is also involved in protein lipoylation via its role as an octanoyl/lipoyl carrier protein intermediate; Belongs to the GcvH family.
 
 
 0.952
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.
  
 0.951
gcvPA
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.
  
 
 0.943
Your Current Organism:
Staphylococcus microti
NCBI taxonomy Id: 569857
Other names: CCM 4903, CCUG 55861, DSM 22147, NCTC 13832, S. microti, Staphylococcus microti Novakova et al. 2010, Staphylococcus sp. CCM 4903, Staphylococcus sp. CCM 4904, strain 4005-LJ(m)
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