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tal protein (Sideroxydans lithotrophicus) - STRING interaction network
"tal" - Transaldolase in Sideroxydans lithotrophicus
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
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[Homology]
Score
talTransaldolase; Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway (317 aa)    
Predicted Functional Partners:
Slit_0014
Transketolase; Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate (672 aa)
   
  0.998
pgi
Glucose-6-phosphate isomerase (548 aa)
 
 
  0.995
zwf
Glucose-6-phosphate 1-dehydrogenase; Catalyzes the oxidation of glucose 6-phosphate to 6- phosphogluconolactone (503 aa)
   
 
  0.972
Slit_2746
2-oxo-acid dehydrogenase E1 subunit, homodimeric type; Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2) (887 aa)
         
  0.963
Slit_0018
Fructose-bisphosphate aldolase, class II, Calvin cycle subtype (354 aa)
   
 
  0.950
Slit_0992
Ketose-bisphosphate aldolase (410 aa)
   
 
  0.944
eno
Enolase; Catalyzes the reversible conversion of 2- phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis (427 aa)
     
  0.933
Slit_1450
Fructose-bisphosphate aldolase (349 aa)
   
 
    0.923
pfp
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 (417 aa)
   
  0.920
fbp
Inositol phosphatase/fructose-16-bisphosphatase (333 aa)
   
 
  0.917
Your Current Organism:
Sideroxydans lithotrophicus
NCBI taxonomy Id: 580332
Other names: S. lithotrophicus, S. lithotrophicus ES-1, Siderooxidans, Siderooxidans lithoautotrophicus, Sideroxydans, Sideroxydans lithotrophicus, Sideroxydans lithotrophicus ES-1, Sideroxydans lithotrophicus str. ES-1, Sideroxydans lithotrophicus strain ES-1, iron-oxidizing lithotroph ES-1
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