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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
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Coexpression
Experiments
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[Homology]
Score
mmgF2-methylisocitrate lyase; Catalyzes the thermodynamically favored C-C bond cleavage of (2R,3S)-2-methylisocitrate to yield pyruvate and succinate. Belongs to the isocitrate lyase/PEP mutase superfamily. Methylisocitrate lyase family. (296 aa)    
Predicted Functional Partners:
prpC
Methylcitrate synthase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Energy metabolism; Belongs to the citrate synthase family.
 
 0.997
prpD
2-methylcitrate dehydratase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Energy metabolism.
 
  
 0.972
prpF
Aconitate isomerase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Energy metabolism.
 
  
 0.956
acnA-I
Aconitate hydratase 1; Catalyzes the isomerization of citrate to isocitrate via cis- aconitate.
  
 0.942
acnB
Bifunctional aconitate hydratase 2 and 2-methylisocitrate dehydratase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Energymetabolism : Anaerobic; Belongs to the aconitase/IPM isomerase family.
  
 
 0.932
sucD
succinyl-CoA synthetase alpha subunit; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.
   
 0.921
aceA
Isocitrate lyase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Energymetabolism : TCA cycle.
  
  
0.920
glcB
Malate synthase G; Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl- CoA) and glyoxylate to form malate and CoA; Belongs to the malate synthase family. GlcB subfamily.
  
 0.919
sucC
succinyl-CoA synthetase, beta subunit glutaryl-CoA synthetase, beta subunit; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
   
 
 0.915
acsA-I
acetyl-CoA synthetase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA; Belongs to the ATP-dependent AMP-binding enzyme family.
  
 
 0.878
Your Current Organism:
Pseudomonas putida KT2440
NCBI taxonomy Id: 160488
Other names: P. putida KT2440, Pseudomonas putida (strain KT2440), Pseudomonas putida str. KT2440
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