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
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[Homology]
Score
gapNThe NADP-dependent glyceraldehyde-3-phosphate dehydrogenase is important as a means of generating NADPH for biosynthetic reactions. It converts the D-glyceraldehyde 3-phosphate to 3-phospho-D-glycerate; Forms a homotetramer and binds a NADP+ per subunit as cofactors; Localized in the cytoplasm; High confidence in function and specificity. (526 aa)    
Predicted Functional Partners:
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.
  
 0.915
pgkA
Phosphoglycerate kinase transfers a phosphate group from 1,3-biphosphoglycerate to ADP, forming ATP and 3-Phosphoglycerate in the seventh step of the glycolysis Embden-Meyerhof pathway). PgkA exists as a monomer containing two nearly equal-sized domains that correspond to the N- and C-termini of the protein. 3-phosphoglycerate binds to the N-terminal, while the nucleotide substrates, MgATP or MgADP, bind to the C-terminal domain of the enzyme; Localized in the cytoplasm; High confidence in function and specificity.
   
 0.914
fbaA
Fructose-bisphosphate aldolase, class II; Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis; Belongs to the class II fructose-bisphosphate aldolase family.
  
 
 0.914
gpmA
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase; Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate.
   
 0.911
fbaB
Fructose-bisphosphate aldolase, class 1; Fructose-bisphosphate aldolase catalyzes the fourth step of the glycolysis (Embden-Meyerhof pathway). It cleaves the hexose D-fructose 1,6-bisphosphate into two trioses sugars: the dihydroxyacetone phosphate (ketone) and the D-glyceraldehyde 3-phosphate (aldehyde); Belongs to the DeoC/LacD aldolase family (Common phosphate binding- site TIM barrel superfamily); Localized in the cytoplasm; High confidence in function and specificity.
  
 
 0.908
dgoA
2-Dehydro-3-deoxy-6-phosphogalactonate aldolase catalyzes the third step of the D-galactonate catabolism: 2-dehydro-3-deoxy-D-galactonate 6-phosphate = pyruvate + D-glyceraldehyde 3-phosphate. Belongs to the class I aldolase whose catalytic mechanism involves the formation of a Schiff-base intermediate between the substrate and the epsilon-amino group of a lysine residue. Localized in the cytoplasm; High confidence in function and specificity.
   
 
 0.907
eda
KHG/KDPG aldolase is a bifunctional enzyme catalyzing the interconversion of 4-hydroxy-2-oxoglutarate into pyruvate and glyoxylate (4-Hydroxy-2-oxoglutarate aldolase activity) and the interconversion of 6-phospho-2-dehydro-3-deoxy-D-gluconate into pyruvate and glyceraldehyde 3-phosphate (Phospho-2-dehydro-3-deoxygluconate aldolase activity). This enzyme is involved in the Entner-Doudoroff pathway and in the glyoxylate and dicarboxylate metabolism; Belongs to the class I aldolase whose catalytic mechanism involves the formation of a Schiff-base intermediate between the substrate and the [...]
   
 
 0.907
gapA
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) catalyzes the sixth step of glycolysis and thus serves to break down glucose for energy and carbon molecules by reversibly catalysing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. Also it plays an important role in gluconeogenesis; Acts as an homotetramer; Localized in the cytoplasm; High confidence in function and specificity.
   
 
 0.906
gapB
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) catalyzes the sixth step of glycolysis and thus serves to break down glucose for energy and carbon molecules by reversibly catalysing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. Also it plays an important role in gluconeogenesis; Acts as an homotetramer; Localized in the cytoplasm; High confidence in function and specificity.
   
 
 0.906
gapC
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) catalyzes the sixth step of glycolysis (Embden-Meyerhof pathway) and thus serves to break down glucose for energy and carbon molecules by reversibly catalysing the oxidation and phosphorylation of D-glyceraldehyde-3- phosphate to 1,3-diphospho-glycerate. Also it plays an important role in gluconeogenesis; Acts as an homotetramer; Localized in the cytoplasm; High confidence in function and specificity.
   
 
 0.906
Your Current Organism:
Zobellia galactanivorans
NCBI taxonomy Id: 63186
Other names: CCUG 47099, CIP 106680, Cytophaga drobachiensis, DSM 12802, Flavobacterium droebachense, Pseudomonas droebachense, Z. galactanivorans, Zobellia galactanivorans corrig. Barbeyron et al. 2001, Zobellia galactanovorans, strain Dsij
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