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
KOY62514.1Phosphoenolpyruvate phosphomutase; Derived by automated computational analysis using gene prediction method: Protein Homology. (285 aa)    
Predicted Functional Partners:
prpC
Catalyzes the synthesis of 2-methylcitrate from propionyl-CoA and oxaloacetate; also catalyzes the condensation of oxaloacetate with acetyl-CoA but with a lower specificity; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.911
prpD
2-methylcitrate dehydratase; Functions in propionate metabolism; involved in isomerization of (2S,3S)-methylcitrate to (2R,3S)-methylisocitrate; also encodes minor aconitase or dehydratase activity; aconitase C; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.872
aceB
Malate synthase; Catalyzes the aldol condensation of glyoxylate with acetyl-CoA to form malate as part of the second step of the glyoxylate bypass and an alternative to the tricarboxylic acid cycle; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.853
KOY63826.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.842
acnA
Aconitate hydratase; Catalyzes the isomerization of citrate to isocitrate via cis- aconitate.
  
 0.831
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.
  
 0.794
KOY61948.1
Acetolactate synthase catalytic subunit; Catalyzes the formation of 2-acetolactate from pyruvate; also known as acetolactate synthase large subunit; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.787
ilvI
Acetolactate synthase 3 catalytic subunit; Catalyzes the formation of 2-acetolactate from pyruvate, leucine sensitive; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.787
adhE
Acetaldehyde dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family.
  
 
 0.782
KOY63403.1
Malic enzyme; NADP-dependent; catalyzes the oxidative decarboxylation of malate to form pyruvate; decarboxylates oxaloacetate; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.734
Your Current Organism:
Photorhabdus heterorhabditis
NCBI taxonomy Id: 880156
Other names: ATCC BAA-2479, DSM 25263, P. heterorhabditis, Photorhabdus heterorhabditis Ferreira et al. 2014, Photorhabdus sp. Q614, Photorhabdus sp. Q614(2009), Photorhabdus sp. SF41, Photorhabdus sp. SF783, strain SF41
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