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
KOH22906.1Malate 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. (192 aa)    
Predicted Functional Partners:
KOH22572.1
Isocitrate lyase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.996
KOH18171.1
Catalyzes the synthesis of acetylphosphate or propionylphosphate from acetyl-CoA or propionyl-CoA and inorganic phosphate; when using propionyl-CoA the enzyme is functioning in the anaerobic pathway catabolizing threonine to propionate; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.973
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; Belongs to the citrate synthase family.
   
 0.966
KOH22025.1
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.
   
 0.953
prpB
2-methylisocitrate lyase; Catalyzes the thermodynamically favored C-C bond cleavage of (2R,3S)-2-methylisocitrate to yield pyruvate and succinate. Belongs to the isocitrate lyase/PEP mutase superfamily. Methylisocitrate lyase family.
  
 
 0.936
KOH17992.1
Catalyzes the formation of fumarate from malate; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.932
mdh
Malate dehydrogenase; Catalyzes the reversible oxidation of malate to oxaloacetate.
   
 0.924
aspA-2
Aspartate ammonia-lyase; Catalyzes the formation of fumarate from aspartate; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.920
KOH22252.1
acetyl-CoA acetyltransferase; Catalyzes the synthesis of acetoacetyl coenzyme A from two molecules of acetyl coenzyme A. It can also act as a thiolase, catalyzing the reverse reaction and generating two-carbon units from the four-carbon product of fatty acid oxidation; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thiolase-like superfamily. Thiolase family.
   
 
 0.919
KOH17526.1
acetyl-CoA acetyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thiolase-like superfamily. Thiolase family.
   
 
 0.919
Your Current Organism:
Vibrio parahaemolyticus
NCBI taxonomy Id: 670
Other names: ATCC 17802, Beneckea parahaemolytica, CAIM 320, CCUG 14474, CCUG 15657, CCUG 4224, CIP 75.2, DSM 10027, IFO 12711, LMG 2850, LMG:2850, NBRC 12711, NCCB 77010, NCCB 77018, NCTC 10903, NRRL B-4167, Oceanomonas parahaemolytica, Pasteurella parahaemolytica, V. parahaemolyticus
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