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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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filled nodes:
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[Homology]
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aceFPyruvate dehydrogenase complex dihydrolipoyllysine-residue acetyltransferase; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). (633 aa)    
Predicted Functional Partners:
lpdA
E3 component of pyruvate and 2-oxoglutarate dehydrogenase complex; catalyzes the oxidation of dihydrolipoamide to lipoamide; Derived by automated computational analysis using gene prediction method: Protein Homology.
 0.999
aceE
E1 component; part of pyruvate dehydrogenase; forms a complex with DlaT and LpdC; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.999
sucA
2-oxoglutarate dehydrogenase subunit E1; Derived by automated computational analysis using gene prediction method: Protein Homology.
 0.995
AMF97636.1
Catalyzes the oxidation of dihydrolipoamide to lipoamide; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.991
pdhB
2-oxoisovalerate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.987
sucC
succinate--CoA ligase 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.
  
 0.975
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.
  
 0.974
AMF99311.1
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.
  
 0.973
pdhA
Pyruvate dehydrogenase (acetyl-transferring) E1 component subunit alpha; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
 
 0.965
AMF96966.1
Catalyzes the synthesis of acetylphosphate or propionylphosphate from acetyl-CoA or propionyl-CoA and inorganic phosphate; when using propionyl-CoA the enzyme is functioning in the anaerobic pathway catabolizing threonine to propionate; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.956
Your Current Organism:
Vibrio harveyi
NCBI taxonomy Id: 669
Other names: ATCC 14126, Achromobacter harveyi, Beneckea harveyi, Beneckea neptuna, CAIM 513, CCUG 28584, CECT 525, CIP 103192, DSM 19623, IFO 15634, LMG 4044, LMG:4044, Lucibacterium harveyi, NBRC 15634, NCCB 80033, NCTC 12970, Photobacterium harveyi, Pseudomonas harveyi, V. harveyi, Vibrio carchariae, Vibrio sp. HENC-01, Vibrio sp. HENC-02, Vibrio sp. PG 001, Vibrio sp. PG 002, Vibrio sp. PG 006, Vibrio sp. PG 007, Vibrio trachuri
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