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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:
some 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
ghrAGlyoxylate/hydroxypyruvate reductase a; Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively. Inactive towards 2-oxo-D-gluconate, 2-oxoglutarate, oxaloacetate and pyruvate. Only D- and L-glycerate are involved in the oxidative activity with NADP. Activity with NAD is very low (312 aa)    
Predicted Functional Partners:
aceA
Isocitrate lyase; Involved in the metabolic adaptation in response to environmental changes. Catalyzes the reversible formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle during growth on fatty acid substrates
     
 0.972
glcB
Malate synthase g; Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl- CoA) and glyoxylate to form malate and CoA
     
 0.969
aceB
Malate synthase A; Protein involved in glyoxylate cycle
     
 0.969
aldA
Lactaldehyde dehydrogenase / glycolaldehyde dehydrogenase; Acts on lactaldehyde as well as other aldehydes
   
 0.965
glcD
Glycolate dehydrogenase, putative fad-linked subunit; Component of a complex that catalyzes the oxidation of glycolate to glyoxylate . Is required for E.coli to grow on glycolate as a sole source of carbon . Is also able to oxidize D-lactate ((R)-lactate) with a similar rate . Does not link directly to O(2), and 2,6-dichloroindophenol (DCIP) and phenazine methosulfate (PMS) can act as artificial electron acceptors in vitro, but the physiological molecule that functions as primary electron acceptor during glycolate oxidation is unknown
    
 0.957
gcl
Tartronate-semialdehyde synthase; Catalyzes the condensation of two molecules of glyoxylate to give 2-hydroxy-3-oxopropanoate (also termed tartronate semialdehyde)
   
 
 0.949
garR
2-hydroxy-3-oxopropionate reductase; Catalyzes the reduction of tatronate semialdehyde to D- glycerate
  
 
 0.947
hyi
Hydroxypyruvate isomerase; Catalyzes the reversible isomerization between hydroxypyruvate and 2-hydroxy-3-oxopropanoate (also termed tartronate semialdehyde). Does not catalyze the isomerization of D-fructose to D- glucose or that of D-xylulose to D-xylose. Also does not catalyze racemization of serine, alanine, glycerate or lactate
    
 0.937
gph
Phosphoglycolate phosphatase; Specifically catalyzes the dephosphorylation of 2- phosphoglycolate (2P-Gly). Is involved in the dissimilation of the intracellular 2-phosphoglycolate formed during the DNA repair of 3'- phosphoglycolate ends, a major class of DNA lesions induced by oxidative stress
  
 
 0.917
glcE
Glycolate dehydrogenase, putative fad-binding subunit; Component of a complex that catalyzes the oxidation of glycolate to glyoxylate . Is required for E.coli to grow on glycolate as a sole source of carbon . Is also able to oxidize D-lactate ((R)-lactate) with a similar rate . Does not link directly to O(2), and 2,6-dichloroindophenol (DCIP) and phenazine methosulfate (PMS) can act as artificial electron acceptors in vitro, but the physiological molecule that functions as primary electron acceptor during glycolate oxidation is unknown
 
  
  0.914
Your Current Organism:
Escherichia coli K12 MG1655
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli K12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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