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
AFK05790.1Fructose-1,6-bisphosphatase, class II; PFAM: Bacterial fructose-1,6-bisphosphatase, glpX-encoded; TIGRFAM: fructose-1,6-bisphosphatase, class II. (337 aa)    
Predicted Functional Partners:
AFK07021.1
PFAM: Transketolase, thiamine diphosphate binding domain; Transketolase, C-terminal domain; Transketolase, pyrimidine binding domain.
   
 0.940
pgi
PFAM: Phosphoglucose isomerase; Belongs to the GPI family.
    
 0.925
AFK06155.1
PFAM: Fructose-bisphosphate aldolase class-II; TIGRFAM: ketose-bisphosphate aldolases; fructose-1,6-bisphosphate aldolase, class II, various bacterial and amitochondriate protist.
  
 
 0.922
tal
Fructose-6-phosphate aldolase, TalC/MipB family; Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway; Belongs to the transaldolase family. Type 3B subfamily.
    
 0.919
AFK08146.1
PFAM: Transaldolase; TIGRFAM: fructose-6-phosphate aldolase, TalC/MipB family.
    
 0.919
pfp
6-phosphofructokinase; Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP- PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
   
 
 0.917
pfp-2
6-phosphofructokinase; Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP- PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
   
 
 0.917
pfkA
6-phosphofructokinase; Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
   
 
 0.917
AFK07437.1
Sugar kinase, ribokinase; PFAM: pfkB family carbohydrate kinase.
    
 0.905
AFK07674.1
Sugar kinase, ribokinase; PFAM: pfkB family carbohydrate kinase.
    
 0.905
Your Current Organism:
Mesotoga prima
NCBI taxonomy Id: 660470
Other names: M. prima MesG1.Ag.4.2, Mesotoga prima MesG1.Ag.4.2, Thermotogales bacterium MesG1.Ag.4.2
Server load: low (18%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.