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
acnA-2Aconitate hydratase; Catalyzes the isomerization of citrate to isocitrate via cis- aconitate. (884 aa)    
Predicted Functional Partners:
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.
 
 0.986
ALO37468.1
Converts isocitrate to alpha ketoglutarate; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.981
ALO37759.1
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.
 
 0.969
rplS
50S ribosomal protein L19; This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site.
   
 
 0.919
rpmB
50S ribosomal protein L28; Required for 70S ribosome assembly; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the bacterial ribosomal protein bL28 family.
   
   0.908
ALO39660.1
PrpF family protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.907
acnB
Aconitate hydratase B; 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.
    
 0.905
rpmF
Some L32 proteins have zinc finger motifs consisting of CXXC while others do not; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the bacterial ribosomal protein bL32 family.
   
   0.904
rpsF
30S ribosomal protein S6; Binds together with S18 to 16S ribosomal RNA.
   
 
 0.900
rpmJ
50S ribosomal protein L36; Smallest protein in the large subunit; similar to what is found with protein L31 and L33 several bacterial genomes contain paralogs which may be regulated by zinc; the protein from Thermus thermophilus has a zinc-binding motif and contains a bound zinc ion; the proteins in this group have the motif; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.900
Your Current Organism:
Alcaligenes faecalis
NCBI taxonomy Id: 511
Other names: A. faecalis, ATCC 8750, Achromobacter sp. ATCC8750, Alcaligenes sp. BP11, CIP 55.84, CIP 60.80, DSM 30030, IAM 12369, IFO 13111, JCM 20522, JCM 20663, NBRC 13111, NCAIM B.01104, NCIMB 8156, NCTC 11953
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