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
tdcEPyruvate formate-lyase; Formate acetyltransferase; catalyzes the formation of formate and acetyl-CoA from pyruvate; Derived by automated computational analysis using gene prediction method: Protein Homology. (764 aa)    
Predicted Functional Partners:
pflA
Pyruvate formate lyase-activating enzyme 1; Activation of pyruvate formate-lyase under anaerobic conditions by generation of an organic free radical, using S- adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine; Belongs to the organic radical-activating enzymes family.
  
 0.973
adhE
Acetaldehyde dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family.
 
 
 0.962
nifJ
Pyruvate-flavodoxin oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.945
pta
Phosphate acetyltransferase; Involved in acetate metabolism. In the N-terminal section; belongs to the CobB/CobQ family.
  
 
 0.925
pykF
Pyruvate kinase; Catalyzes the formation of phosphoenolpyruvate from pyruvate; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.868
pykA
Pyruvate kinase; Catalyzes the formation of phosphoenolpyruvate from pyruvate; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.841
maeB
Malic enzyme; NADP-dependent; catalyzes the oxidative decarboxylation of malate to form pyruvate; decarboxylates oxaloacetate; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.826
gltA
Type II enzyme; in Escherichia coli this enzyme forms a trimer of dimers which is allosterically inhibited by NADH and competitively inhibited by alpha-ketoglutarate; allosteric inhibition is lost when Cys206 is chemically modified which also affects hexamer formation; forms oxaloacetate and acetyl-CoA and water from citrate and coenzyme A; functions in TCA cycle, glyoxylate cycle and respiration; enzyme from Helicobacter pylori is not inhibited by NADH; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the citrate synthase family.
     
 0.777
tdcB
Threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.
  
 
 0.736
maeA
Malate dehydrogenase; Malic enzyme; oxaloacetate-decarboxylating; NAD-dependent; catalyzes the formation of pyruvate form malate; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.723
Your Current Organism:
Yersinia ruckeri
NCBI taxonomy Id: 29486
Other names: ATCC 29473, CCM 6093, CCUG 14190, CDC 2396-61, CIP 82.80, DSM 18506, JCM 15110, JCM 2429, NCIB 2194, NCIMB 2194, NCTC 12986, Y. ruckeri
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