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
ppsAPhosphoenolpyruvate synthase; Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate; Belongs to the PEP-utilizing enzyme family. (802 aa)    
Predicted Functional Partners:
ddh
NAD-dependent 2-hydroxyacid dehydrogenases are enzymes which seem to be specific for the D-isomer of their substrate. these enzymes are composed of a substrate-binding domain and a NAD-binding domain (Rossman fold); Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family; Localized in the cytoplasm; High confidence in function and specificity.
    
 0.967
maeB
Bifunctional protein: Malic enzyme (N-terminal domain, 1 to 550) and Phosphate acetyl/butaryl transferase (C-terminal domain, 550 to 765); High confidence in function and specificity.
  
 
 0.942
pycA
Pyruvate carboxylase; Catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second.
  
 
 0.930
pykA
Pyruvate kinase (PK) catalyzes the final step in glycolysis (Embden-Meyerhof pathway), the conversion of phosphoenolpyruvate to pyruvate with concomitant phosphorylation of ADP to ATP. PK forms a homotetramer and requires both magnesium and potassium ions for its activity. PK helps control the rate of glycolysis, along with phosphofructokinase and hexokinase. PK possesses allosteric sites for numerous effectors; Localized in the cytoplasm; High confidence in function and specificity.
    
 0.925
enoA
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.
    
 0.925
ppcA
Phosphoenolpyruvate carboxylase; Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
     
 0.925
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.
  
 
 0.920
pdhA
Pyruvate dehydrogenase, E1 component subunit alpha; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
    
 0.914
pdhB
Pyruvate dehydrogenase, E1 component subunit beta; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.
    
 0.913
pckA2
Phosphoenolpyruvate carboxykinase [ATP]; Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.
     
 0.912
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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