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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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[Homology]
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AKL37067.1Bifunctional 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. (866 aa)    
Predicted Functional Partners:
icd
Converts isocitrate to alpha ketoglutarate; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.974
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.
  
 
 0.958
gltA-2
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.
  
 
 0.958
acnA
Aconitate hydratase; Catalyzes the isomerization of citrate to isocitrate via cis- aconitate.
    
0.934
aceA
Isocitrate lyase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.919
AKL38133.1
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.
  
  
 
0.901
sucA
2-oxoglutarate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
  
 0.769
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.
  
  
 0.764
AKL37422.1
Dihydrolipoamide succinyltransferase; E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2- oxoglutarate to succinyl-CoA and CO(2).
  
  
 0.724
nuoC
NADH:ubiquinone oxidoreductase; 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.
   
  
 0.716
Your Current Organism:
Klebsiella oxytoca
NCBI taxonomy Id: 571
Other names: ATCC 13182, Bacillus oxytocus perniciosus, CCUG 15717, CIP 103434, DSM 5175, IAM 14201, K. oxytoca, Klebsiella sp. CECRI-24/07, Klebsiella sp. MN9SED2, LMG 3055, LMG:3055, NBRC 102593, NBRC 105695, NCTC 13727, strain 479-2
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