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lipB protein (Sideroxydans lithotrophicus) - STRING interaction network
"lipB" - Lipoate-protein ligase B in Sideroxydans lithotrophicus
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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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lipBLipoate-protein ligase B; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate (215 aa)    
Predicted Functional Partners:
lipA
Lipoic acid synthetase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives (311 aa)
 
  0.999
acpP
Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis (77 aa)
     
  0.960
gcvH
Glycine cleavage system H protein; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein (129 aa)
   
  0.958
Slit_0354
Hypothetical protein (87 aa)
     
  0.958
Slit_1532
3-oxoacyl-ACP synthase II; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP (410 aa)
     
    0.825
Slit_0447
Beta-ketoacyl synthase; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP (413 aa)
     
    0.825
Slit_0356
Beta-ketoacyl synthase (353 aa)
     
    0.825
Slit_0350
Beta-ketoacyl synthase (397 aa)
     
    0.825
Slit_1799
Short-chain dehydrogenase/reductase SDR (261 aa)
   
 
  0.823
gcvP
Glycine dehydrogenase; The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein (949 aa)
 
   
  0.787
Your Current Organism:
Sideroxydans lithotrophicus
NCBI taxonomy Id: 580332
Other names: S. lithotrophicus, S. lithotrophicus ES-1, Siderooxidans, Siderooxidans lithoautotrophicus, Sideroxydans, Sideroxydans lithotrophicus, Sideroxydans lithotrophicus ES-1, Sideroxydans lithotrophicus str. ES-1, Sideroxydans lithotrophicus strain ES-1, iron-oxidizing lithotroph ES-1
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