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
aceEPyruvate dehydrogenase; Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). (882 aa)    
Predicted Functional Partners:
aceF
Dihydrolipoamide acetyltransferase; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
 0.999
PA3415
Probable dihydrolipoamide acetyltransferase; Product name confidence: Class 3 (Function proposed based on presence of conserved amino acid motif, structural feature or limited sequence similarity to an experimentally studied gene).
 
 0.980
PA4152
Probable hydrolase; Product name confidence: Class 3 (Function proposed based on presence of conserved amino acid motif, structural feature or limited sequence similarity to an experimentally studied gene).
  
 0.976
lpdG
Lipoamide dehydrogenase-glc; The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
  
 
 0.970
pykA
Pyruvate kinase II; Product name confidence: Class 2 (High similarity to functionally studied protein); Belongs to the pyruvate kinase family.
  
 
 0.963
lpd3
Dihydrolipoamide dehydrogenase 3; LPD-3 may substitute for lipoamide dehydrogenase of the 2- oxoglutarate dehydrogenase and pyruvate multienzyme complexes when the latter is inactive or missing; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
  
 
 0.953
PA5435
Probable transcarboxylase subunit; Product name confidence: Class 3 (Function proposed based on presence of conserved amino acid motif, structural feature or limited sequence similarity to an experimentally studied gene).
  
 
 0.947
PA5436
Probable biotin carboxylase subunit of a transcarboxylase; This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
     
 0.947
lpdV
Lipoamide dehydrogenase-Val; The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity); Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
  
 
 0.945
pykF
Pyruvate kinase I; Product name confidence: Class 2 (High similarity to functionally studied protein); Belongs to the pyruvate kinase family.
  
 
 0.943
Your Current Organism:
Pseudomonas aeruginosa
NCBI taxonomy Id: 208964
Other names: P. aeruginosa PAO1, Pseudomonas aeruginosa PAO1, Pseudomonas sp. PAO1
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