close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING • newly available directed regulatory networks • a new typed view showing functional, physical, and regulatory edges in one network • new clustering options and cluster-based layouts • … and much more!
Explore STRING v12.5 →
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
fbaBFructose-bisphosphate aldolase class I; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (307 aa)    
Predicted Functional Partners:
fbp-2
Fructose-1-6-bisphosphatase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the FBPase class 1 family.
    
 0.973
tktA
Transketolase; Function of homologous gene experimentally demonstrated in an other organism; enzyme.
  
 
 0.936
talC
Transaldolase, putative Fructose-6-phosphate aldolase; Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway; Belongs to the transaldolase family. Type 3B subfamily.
  
 
 0.932
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.
  
 
 0.928
gapA
Glyceraldehyde-3-phosphate dehydrogenase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
    
 0.927
pfkA
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.
    
 0.920
NIDE4287
Putative 6-phosphofructokinase (modular protein); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.
    
 0.920
fbpV
Fructose-1,6-bisphosphatase, class V; Catalyzes two subsequent steps in gluconeogenesis: the aldol condensation of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3- phosphate (GA3P) to fructose-1,6-bisphosphate (FBP), and the dephosphorylation of FBP to fructose-6-phosphate (F6P).
     
 0.916
deoC
Deoxyribose-phosphate aldolase; Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5- phosphate; Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.
    
 0.913
manB/pgm
Bifunctional Phosphoglucomutase/Phosphomannomutase; Function of strongly homologous gene; enzyme.
 
  
 0.906
Your Current Organism:
Nitrospira defluvii
NCBI taxonomy Id: 330214
Other names: Candidatus Nitrospira defluvii, LMG 27402, LMG:27402, N. defluvii, NCIMB 14950, strain A17
Server load: low (22%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.