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JG24_19045 protein (Klebsiella pneumoniae) - STRING interaction network
"JG24_19045" - Protein acetyltransferase in Klebsiella pneumoniae
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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[Homology]
Score
JG24_19045Protein acetyltransferase; Catalyzes the acetylation of lysine; Derived by automated computational analysis using gene prediction method- Protein Homology (883 aa)    
Predicted Functional Partners:
sucD
Succinate--CoA ligase [ADP-forming] subunit alpha; 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 alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit (289 aa)
   
 
  0.951
JG24_16630
Derived by automated computational analysis using gene prediction method- Protein Homology (1171 aa)
   
 
  0.929
JG24_10255
Pyruvate-flavodoxin oxidoreductase; Derived by automated computational analysis using gene prediction method- Protein Homology (1175 aa)
   
 
  0.928
JG24_17900
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 (715 aa)
   
   
  0.872
JG24_27415
Acetyl-coenzyme A synthetase; Acs; catalyzes the conversion of acetate and CoA to acetyl-CoA; Derived by automated computational analysis using gene prediction method- Protein Homology (652 aa)
 
   
  0.858
JG24_22345
Derived by automated computational analysis using gene prediction method- Protein Homology (473 aa)
   
   
  0.853
JG24_06080
Citrate 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 citrate [...] (427 aa)
   
 
  0.825
JG24_04770
Citrate synthase (Si); 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 (434 aa)
   
 
  0.825
JG24_19040
Uncharacterized protein; Derived by automated computational analysis using gene prediction method- Protein Homology (232 aa)
              0.821
JG24_18510
NADP-dependent malic enzyme; NADP-dependent; catalyzes the oxidative decarboxylation of malate to form pyruvate; decarboxylates oxaloacetate; Derived by automated computational analysis using gene prediction method- Protein Homology (759 aa)
   
   
  0.803
Your Current Organism:
Klebsiella pneumoniae
NCBI taxonomy Id: 573
Other names: ATCC 13883, Bacillus pneumoniae, Bacterium pneumoniae crouposae, CCUG 225, CIP 82.91, DSM 30104, HAMBI 450, Hyalococcus pneumoniae, IFO 14940, K. pneumoniae, Klebsiella pneumoniae, Klebsiella sp. M-AI-2, Klebsiella sp. PB12, Klebsiella sp. RCE-7, LMG 2095, NBRC 14940, NCTC 9633
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