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
acnB_2Bifunctional 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. (868 aa)    
Predicted Functional Partners:
icd_1
Converts isocitrate to alpha ketoglutarate; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.992
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.
  
 
 0.985
mdh_2
Malate dehydrogenase; Catalyzes the reversible oxidation of malate to oxaloacetate.
  
  
 0.795
sucC
succinyl-CoA synthetase subunit beta; Catalyzes the interconversion of succinyl-CoA and succinate; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.767
sucA_2
2-oxoglutarate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
  
 0.754
frdA_1
Part of four member fumarate reductase enzyme complex FrdABCD which catalyzes the reduction of fumarate to succinate during anaerobic respiration; FrdAB are the catalytic subcomplex consisting of a flavoprotein subunit and an iron-sulfur subunit, respectively; FrdCD are the membrane components which interact with quinone and are involved in electron transfer; the catalytic subunits are similar to succinate dehydrogenase SdhAB; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.547
prfB
Peptide chain release factor 2; Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA.
      
 0.499
fabA
3-hydroxydecanoyl-ACP dehydratase; Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E- (2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length.
      
 0.489
frdB_2
Fumarate reductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.488
torZ_4
Catalyzes the reduction of trimethylamine-N-oxide to form trimethylamine; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.487
Your Current Organism:
Mannheimia haemolytica
NCBI taxonomy Id: 75985
Other names: ATCC 33396, CCUG 12392, CCUG 408, CIP 103426, DSM 10531, M. haemolytica, NCTC 9380, Pasteurella haemolytica, strain J.A. Watt 1266AB
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