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JG24_07575 protein (Klebsiella pneumoniae) - STRING interaction network
"JG24_07575" - Gamma-glutamyl-aminobutyraldehyde dehydrogenase in Klebsiella pneumoniae
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second shell of interactors
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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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Score
JG24_07575Gamma-glutamyl-aminobutyraldehyde dehydrogenase; Catalyzes the formation of succinate from succinate semialdehyde; NADP dependent; Derived by automated computational analysis using gene prediction method- Protein Homology (482 aa)    
Predicted Functional Partners:
JG24_24050
Gamma-aminobutyrate-alpha-ketoglutarate aminotransferase; Catalyzes the formation of succinate semialdehyde and glutamate from 4-aminobutanoate and 2-oxoglutarate; Derived by automated computational analysis using gene prediction method- Protein Homology (421 aa)
 
  0.962
JG24_03450
Gamma-aminobutyrate-alpha-ketoglutarate aminotransferase; Derived by automated computational analysis using gene prediction method- Protein Homology (427 aa)
 
  0.962
JG24_29015
2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the HpcH/HpaI aldolase family (265 aa)
       
  0.941
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)
   
 
  0.869
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)
   
 
  0.858
JG24_23110
Oxidizes malate to oxaloacetate; Derived by automated computational analysis using gene prediction method- Protein Homology (312 aa)
   
  0.831
JG24_28925
Succinate-semialdehyde dehydrogenase [NAD] Succinate-semialdehyde dehydrogenase [NADP+]; In Escherichia coli this enzyme appears to be an NAD+/NADP+-dependent succinate semialdehyde dehydrogenase; Derived by automated computational analysis using gene prediction method- Protein Homology (456 aa)
   
   
 
0.830
fumC
Fumarate hydratase class II; Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate; Belongs to the class-II fumarase/aspartase family. Fumarase subfamily (466 aa)
     
  0.828
JG24_17600
Probable malate-quinone oxidoreductase; Derived by automated computational analysis using gene prediction method- Protein Homology (544 aa)
     
 
  0.821
JG24_11240
Probable malate-quinone oxidoreductase; Derived by automated computational analysis using gene prediction method- Protein Homology (551 aa)
     
 
  0.821
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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