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
KJJ37658.1PEP carboxykinase; PEP carboxylase; PEPCK; catalyzes the phosphorylation and decarboxylation of oxaloacetate to form phosphoenolpyruvate using ATP; Derived by automated computational analysis using gene prediction method: Protein Homology. (533 aa)    
Predicted Functional Partners:
eno
Enolase; Catalyzes the formation of phosphoenolpyruvate from 2-phospho-D-glycerate in glycolysis; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.958
KJJ37989.1
Malate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.958
KJJ37762.1
Pyruvate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.954
KJJ39472.1
methylmalonyl-CoA mutase; MDM; functions in conversion of succinate to propionate; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.925
gltA
Type II enzyme; in Escherichia coli this enzyme forms a trimer of dimers which is allosterically inhibited by NADH and competitively inhibited by alpha-ketoglutarate; allosteric inhibition is lost when Cys206 is chemically modified which also affects hexamer formation; forms oxaloacetate and acetyl-CoA and water from citrate and coenzyme A; functions in TCA cycle, glyoxylate cycle and respiration; enzyme from Helicobacter pylori is not inhibited by NADH; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.919
KJJ39411.1
acetyl-CoA synthetase; Acs; catalyzes the conversion of acetate and CoA to acetyl-CoA; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.917
KJJ38553.1
Pyruvate kinase; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.917
KJJ39176.1
Malate:quinone oxidoreductase; Malate dehydrogenase; catalyzes the oxidation of malate to oxaloacetate; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.915
KJJ37802.1
Pyruvate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.913
KJJ37763.1
Pyruvate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.909
Your Current Organism:
Aequorivita vladivostokensis
NCBI taxonomy Id: 171194
Other names: A. vladivostokensis, Aequorivita vladivostokensis (Nedashkovskaya et al. 2003) Hahnke et al. 2016, JCM 11732, KMM 3516, NBRC 16718, Vitellibacter vladivostokensis, Vitellibacter vladivostokensis Nedashkovskaya et al. 2003
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