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
gcvPAGlycine 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. (458 aa)    
Predicted Functional Partners:
EH31_08285
Aminomethyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.999
gcvH
Glycine 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.
 0.999
EH31_08300
Glycine dehydrogenase; Acts in conjunction with GvcH to form H-protein-S-aminomethyldihydrolipoyllysine from glycine; forms a heterodimer with subunit 1 to form the P protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 0.999
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.
 
 
 0.977
EH31_01890
E3 component of alpha keto acid dehydrogenase complexes LpdC; forms a homodimer; binds one molecule of FAD monomer; catalyzes NAD+-dependent oxidation of dihydrolipoyl cofactors that are covalently linked to the E2 component; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.967
EH31_03665
Catalyzes the oxidation of dihydrolipoamide to lipoamide; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.967
EH31_15475
Glutamate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.951
EH31_12940
Threonine aldolase; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.931
EH31_00425
Catalyzes the formation of 5-aminolevulinate from succinyl-CoA and glycine; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.919
purQ
Phosphoribosylformylglycinamidine synthase; Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP- dependent manner. PurS interacts with PurQ and PurL and is thought to assist in [...]
  
 
  0.886
Your Current Organism:
Erythrobacter longus
NCBI taxonomy Id: 1044
Other names: ATCC 33941, CIP 104268, DSM 6997, E. longus, IFO 14126, JCM 6170, NBRC 14126, strain OCh101
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