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
KOH24740.1Proline:sodium symporter PutP; Involved in the sodium dependent uptake of proline; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family. (497 aa)    
Predicted Functional Partners:
KOH19672.1
Carbon starvation protein CstA; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
    0.813
KOH24739.1
1-pyrroline-5-carboxylate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.778
KOH24884.1
Flagellar biosynthesis protein FliS; Derived by automated computational analysis using gene prediction method: Protein Homology.
      
 0.681
KOH22471.1
Hypothetical protein; Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
  
    0.618
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.
   
  
 0.566
KOH17814.1
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.
   
  
 0.566
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.
  
  
 0.547
prpE
Catalyzes the formation of propionyl-CoA using propionate as a substrate; PrpE from Ralstonia solanacearum can produce acetyl-, propionyl-, butyryl- and acrylyl-coenzyme A, and Salmonella enterica produces propionyl- and butyryl-coenzyme A; not expressed in Escherichia coli when grown on propionate/minimal media; ATP-dependent; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.547
tet(34)
Xanthine-guanine phosphoribosyltransferase; Acts on guanine, xanthine and to a lesser extent hypoxanthine; Belongs to the purine/pyrimidine phosphoribosyltransferase family. XGPT subfamily.
   
  
 0.520
KOH18247.1
Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP which is metabolically less costly than a de novo synthesis; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
  
 0.520
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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