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
AEX84712.1Fructose-1-phosphate kinase/fructose-6-phosphate kinase; PFAM: pfkB family carbohydrate kinase; TIGRFAM: hexose kinase, 1-phosphofructokinase family. (318 aa)    
Predicted Functional Partners:
AEX85824.1
PFAM: Fructose-bisphosphate aldolase class-II; TIGRFAM: ketose-bisphosphate aldolases; fructose-1,6-bisphosphate aldolase, class II, various bacterial and amitochondriate protist.
  
 
 0.941
AEX84815.1
PFAM: pfkB family carbohydrate kinase; TIGRFAM: hexose kinase, 1-phosphofructokinase family.
  
  
 
0.928
pfkA
6-phosphofructokinase; Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
     
 0.905
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.
     
 0.905
pfp-2
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.
     
 0.905
AEX86162.1
6-phosphofructokinase; Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis; Belongs to the phosphofructokinase type A (PFKA) family.
     
 0.905
AEX85621.1
Fructose-1,6-bisphosphatase, class II; PFAM: Bacterial fructose-1,6-bisphosphatase, glpX-encoded; TIGRFAM: fructose-1,6-bisphosphatase, class II.
     
 0.902
gyrB
Type IIA topoisomerase (DNA gyrase/topo II, topoisomerase IV), B subunit; A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA stran [...]
     
 0.803
AEX84714.1
MiaB-like tRNA modifying enzyme; PFAM: Radical SAM superfamily; Uncharacterized protein family UPF0004; TIGRFAM: MiaB-like tRNA modifying enzyme; radical SAM methylthiotransferase, MiaB/RimO family.
       0.790
AEX84715.1
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase; PFAM: Aminotransferase class IV.
       0.790
Your Current Organism:
Marinitoga piezophila
NCBI taxonomy Id: 443254
Other names: M. piezophila KA3, Marinitoga piezophila KA3, Marinitoga piezophila str. KA3, Marinitoga piezophila strain KA3, Thermotogales sp. KA3
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