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
Databases
Textmining
[Homology]
Score
AGA29236.1Folate-binding protein YgfZ; PFAM: Aminomethyltransferase folate-binding domain; Glycine cleavage T-protein C-terminal barrel domain; TIGRFAM: folate-binding protein YgfZ; Belongs to the GcvT family. (353 aa)    
Predicted Functional Partners:
gcvH
Glycine cleavage system H protein; 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.
 
 0.995
gcvPB
Glycine cleavage system protein P; 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.
 
 
 0.937
gcvPA
Glycine cleavage system protein P; 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.
 
  
 0.932
sucC
succinyl-CoA synthetase, beta subunit; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
  
  
 0.798
AGA29235.1
PFAM: Uncharacterized conserved protein (DUF2088).
       0.794
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.
 
 
 0.741
gcvT
Glycine cleavage system T protein; The glycine cleavage system catalyzes the degradation of glycine.
  
     0.738
AGA30624.1
Pyruvate/2-oxoglutarate dehydrogenase complex, dehydrogenase component beta subunit; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.
     
 0.673
AGA31346.1
Glycine oxidase ThiO; PFAM: FAD dependent oxidoreductase; TIGRFAM: glycine oxidase ThiO.
 
 
 0.673
AGA29355.1
Glycine oxidase ThiO; PFAM: FAD dependent oxidoreductase; TIGRFAM: glycine oxidase ThiO.
 
 
 0.663
Your Current Organism:
Singulisphaera acidiphila
NCBI taxonomy Id: 886293
Other names: S. acidiphila DSM 18658, Singulisphaera acidiphila DSM 18658, Singulisphaera acidiphila MOB10, Singulisphaera acidiphila str. DSM 18658, Singulisphaera acidiphila strain DSM 18658
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.