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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
gapGlyceraldehyde-3-phosphate dehydrogenase; NAD-dependent; catalyzes the formation of 3-phospho-D-glyceroyl phosphate from D-glyceraldehyde 3-phosphate; active during glycolysis; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. (348 aa)    
Predicted Functional Partners:
tpiA
Triose-phosphate 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.
 0.999
pgk
Phosphoglycerate kinase; Converts 3-phospho-D-glycerate to 3-phospho-D-glyceroyl phosphate during the glycolysis pathway; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the phosphoglycerate kinase family.
 0.999
eno
Enolase; Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis; Belongs to the enolase family.
 
 0.988
kbaY-2
Tagatose-bisphosphate aldolase; Catalyzes the reversible reaction of dihydroxyacetone phosphate with glyceraldehyde 3-phosphate to produce tagatose 1,6-bisphosphate; in enteric bacteria there are two D-tagatose 1,6-bisphosphate-specific aldolases: KbaY (also called AgaY), involved in catabolism of N-acetyl-galactosamine and D-galactosamine, and GatY which is part of the galactitol catabolism pathway; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.982
pyk
Pyruvate kinase; Catalyzes the formation of phosphoenolpyruvate from pyruvate; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.962
pgi
Glucose-6-phosphate isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the GPI family.
  
 
 0.961
KZE52325.1
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.
 
 0.946
zwf
Glucose-6-phosphate dehydrogenase; Catalyzes the oxidation of glucose 6-phosphate to 6- phosphogluconolactone.
  
 0.945
kbaY
Tagatose-bisphosphate aldolase; Catalyzes the reversible reaction of dihydroxyacetone phosphate with glyceraldehyde 3-phosphate to produce tagatose 1,6-bisphosphate; in enteric bacteria there are two D-tagatose 1,6-bisphosphate-specific aldolases: KbaY (also called AgaY), involved in catabolism of N-acetyl-galactosamine and D-galactosamine, and GatY which is part of the galactitol catabolism pathway; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.939
gapA
Glyceraldehyde-3-phosphate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
  
  
 
0.931
Your Current Organism:
Brevibacillus parabrevis
NCBI taxonomy Id: 54914
Other names: ATCC 10027, B. parabrevis, Bacillus parabrevis, CIP 103840, DSM 8376, IFO 12334, JCM 8506, LMG 15971, LMG:15971, NBRC 12334, NCIMB 13346, NRRL NRS-605, NRRL NRS-815
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