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
ALO67897.1Isocitrate dehydrogenase; NADP-specific, catalyzes the formation of 2-oxoglutarate from isocitrate or oxalosuccinate; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the monomeric-type IDH family. (740 aa)    
Predicted Functional Partners:
ALO66161.1
Ferredoxin; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
  
  
 0.846
acnA
Aconitate hydratase; Catalyzes the conversion of citrate to isocitrate; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.824
mdh
Malate dehydrogenase; Catalyzes the reversible oxidation of malate to oxaloacetate. Belongs to the LDH/MDH superfamily. MDH type 2 family.
  
  
 0.797
ALO65450.1
L-lactate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.678
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.
  
  
 0.568
ALO67497.1
Citrate synthase/methylcitrate synthase; Catalyzes the formation of citrate from acetyl-CoA and oxaloacetate; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.568
ALO68551.1
Glutamate synthase subunit alpha; Derived by automated computational analysis using gene prediction method: Protein Homology.
      
 0.556
sucC
succinyl-CoA synthetase subunit beta; 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.
  
  
 0.533
ALO67898.1
Ferritin; Iron-storage protein.
       0.510
sucD
succinyl-CoA synthetase subunit alpha; 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.
  
  
 0.508
Your Current Organism:
Arthrobacter alpinus
NCBI taxonomy Id: 656366
Other names: A. alpinus, Arthrobacter alpinus Zhang et al. 2010, Arthrobacter sp. A3, Arthrobacter sp. S6-3, CGMCC 1.8950, DSM 22274, strain S6-3
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