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
pfkA1_16-phosphofructokinase 1; 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. (421 aa)    
Predicted Functional Partners:
pgi
Glucose-6-phosphate isomerase; Belongs to the GPI family.
  
 0.971
fba
Fructose-bisphosphate aldolase.
  
 
 0.923
tkt
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.
  
 
 0.914
pfp_1
Pyrophosphate--fructose 6-phosphate 1-phosphotransferase; 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.
  
  
 
0.913
talB
Transaldolase B.
  
 
 0.912
fbaB
Fructose-bisphosphate aldolase class 1.
    
 0.910
lacC
Tagatose-6-phosphate kinase.
     
 0.909
pfkA1_2
6-phosphofructokinase 1; 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.
  
  
 
0.909
gmuF
Putative mannose-6-phosphate isomerase GmuF.
    
 0.907
srlD
Sorbitol-6-phosphate 2-dehydrogenase.
    
 0.906
Your Current Organism:
Anaerohalosphaera lusitana
NCBI taxonomy Id: 1936003
Other names: A. lusitana, Anaerohalosphaera lusitana Pradel et al., DSM 103484, JCM 31926, KCTC 15600, Phycisphaerae bacterium ST-NAGAB-D1, strain ST-NAGAB-D1
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