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
prpB2-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. (294 aa)    
Predicted Functional Partners:
KRG65330.1
Catalyzes the synthesis of 2-methylcitrate from propionyl-CoA and oxaloacetate; also catalyzes the condensation of oxaloacetate with acetyl-CoA but with a lower specificity; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.970
KRG65332.1
Citrate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.867
KRG65329.1
Aconitate hydratase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.795
KRG62896.1
Bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Catalyzes the conversion of citrate to isocitrate and the conversion of 2-methylaconitate to 2-methylisocitrate; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the aconitase/IPM isomerase family.
     
 0.793
KRG65489.1
Malate synthase; Catalyzes the aldol condensation of glyoxylate with acetyl-CoA to form malate as part of the second step of the glyoxylate bypass and an alternative to the tricarboxylic acid cycle; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.745
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.
  
 0.724
acsA
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.
  
 
 0.722
KRG63774.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.685
KRG65327.1
3-methylitaconate isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.662
KRG64773.1
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.
    
 0.643
Your Current Organism:
Stenotrophomonas humi
NCBI taxonomy Id: 405444
Other names: DSM 18929, LMG 23959, LMG:23959, S. humi, Stenotrophomonas humi Heylen et al. 2007, Stenotrophomonas sp. R-32729, strain R-32729
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