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aceK protein (Idiomarina loihiensis) - STRING interaction network
"aceK" - Isocitrate dehydrogenase kinase/phosphatase in Idiomarina loihiensis
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Known Interactions
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experimentally determined
Predicted Interactions
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gene co-occurrence
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textmining
co-expression
protein homology
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aceKIsocitrate dehydrogenase kinase/phosphatase; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation (564 aa)    
Predicted Functional Partners:
aceA
Isocitrate lyase (445 aa)
 
   
  0.851
aceB
Malate synthase (527 aa)
 
   
  0.723
IL0606
LysR family transcriptional regulator (311 aa)
              0.612
gdhA
Glutamate dehydrogenase (450 aa)
       
    0.599
acnA
Aconitase A; Catalyzes the isomerization of citrate to isocitrate via cis-aconitate (889 aa)
     
 
    0.576
IL1425
Aconitate hydratase; Catalyzes the isomerization of citrate to isocitrate via cis-aconitate (864 aa)
     
 
    0.576
IL1864
3-oxoacyl-ACP synthase; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched- chain and/or straight-chain of fatty acids (362 aa)
           
  0.552
IL1342
3-oxoacyl-ACP synthase; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched- chain and/or straight-chain of fatty acids (320 aa)
           
  0.552
fadA
3-ketoacyl-CoA thiolase; Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed (387 aa)
         
  0.549
fadJ
Multifunctional fatty acid oxidation complex subunit alpha; Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3-hydroxyacyl-CoA dehydrogenase activities (708 aa)
           
  0.546
Your Current Organism:
Idiomarina loihiensis
NCBI taxonomy Id: 283942
Other names: I. loihiensis, I. loihiensis L2TR, Idiomarina loihiensis, Idiomarina loihiensis Donachie et al. 2003, Idiomarina loihiensis L2TR, Idiomarina loihiensis str. L2TR, Idiomarina loihiensis strain L2TR
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