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
VC_0478Fructose-bisphosphate aldolase, class II; Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis; Belongs to the class II fructose-bisphosphate aldolase family. (358 aa)    
Predicted Functional Partners:
pgk
Phosphoglycerate kinase; Similar to SP:P11665 PID:41422 PID:882455 GB:U00096 PID:1789294; identified by sequence similarity; putative; Belongs to the phosphoglycerate kinase family.
  
 0.990
tpiA
Triosephosphate isomerase; Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D- glyceraldehyde-3-phosphate (G3P); Belongs to the triosephosphate isomerase family.
 
 
 0.975
fadJ
Fatty oxidation complex, alpha subunit; Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3- hydroxyacyl-CoA dehydrogenase activities; In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.
   
 0.962
fadB
Fatty oxidation complex, alpha subunit; Involved in the aerobic and anaerobic degradation of long- chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
   
 0.962
eno
Enolase; Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
  
 0.956
pgi
Glucose-6-phosphate isomerase; Similar to SP:P11537 GB:X15196 PID:396360 PID:42377 GB:U00096; identified by sequence similarity; putative.
  
 
 0.955
VC_1069
Glyceraldehyde 3-phosphate dehydrogenase; Similar to GB:L07499 SP:P34918 PID:410113; identified by sequence similarity; putative; Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
  
 0.936
VC_2000
Glyceraldehyde 3-phosphate dehydrogenase; Similar to GB:X02662 SP:P06977 GB:M66870 GB:M66871 GB:M66872; identified by sequence similarity; putative; Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
  
 0.936
VC_A0843
Glyceraldehyde 3-phosphate dehydrogenase; Similar to GP:3170587; identified by sequence similarity; putative; Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
  
 0.935
pfkA
6-phosphofructokinase, isozyme I; Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
 
 
 0.930
Your Current Organism:
Vibrio cholerae
NCBI taxonomy Id: 243277
Other names: V. cholerae O1 biovar El Tor str. N16961, Vibrio cholerae El Tor N16961, Vibrio cholerae O1 biovar El Tor str. N16961, Vibrio cholerae O1 biovar eltor str. N16961, Vibrio cholerae serotype O1 biotype El Tor strain N16961, Vibrio cholerae serotype O1 biotype ElTor strain N16961
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.