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
AOX16171.1Aconitate hydratase; Catalyzes the isomerization of citrate to isocitrate via cis- aconitate. (897 aa)    
Predicted Functional Partners:
gltA
Citrate (Si)-synthase; 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 cit [...]
  
 0.977
gltA-2
Citrate (Si)-synthase; 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 cit [...]
  
 0.977
AOX16549.1
Isocitrate dehydrogenase; Catalyzes the formation of 2-oxoglutarate from isocitrate; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.929
AOX16957.1
Isocitrate dehydrogenase; Catalyzes the formation of 2-oxoglutarate from isocitrate; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.929
AOX16544.1
Aconitate hydratase; Catalyzes the isomerization of citrate to isocitrate via cis- aconitate.
  
  
 
0.900
AOX16173.1
Amino acid ABC transporter permease; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.858
AOX16305.1
Superoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family.
   
 
 0.821
glnQ
Similar to ATP-binding component of ABC transporters; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.810
AOX16553.1
Succinate dehydrogenase iron-sulfur subunit; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
  
 
 0.733
nuoC
NADH-quinone oxidoreductase subunit C/D; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; In the C-terminal section; belongs to the complex I 49 kDa subunit family.
  
 
 0.732
Your Current Organism:
Kozakia baliensis
NCBI taxonomy Id: 153496
Other names: DSM 14400, IFO 16664, JCM 11301, K. baliensis, Kozakia baliensis Lisdiyanti et al. 2002, NBRC 16664, NRIC 0488, strain Yo-3
Server load: low (8%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.