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Slit_0035 protein (Sideroxydans lithotrophicus) - STRING interaction network
"Slit_0035" - Methionine biosynthesis protein MetW in Sideroxydans lithotrophicus
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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Slit_0035Methionine biosynthesis protein MetW (200 aa)    
Predicted Functional Partners:
metX
Homoserine O-acetyltransferase; Involved in the methionine biosynthesis. Catalyzes the transfer of the acetyl group from acetyl-CoA to the hydroxyl group of L-homoserine to yield O-acetyl-L-homoserine (377 aa)
   
  0.997
nuoB
NADH-quinone oxidoreductase, B subunit; NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (159 aa)
     
    0.935
nuoI
NADH-quinone oxidoreductase, chain I; NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (162 aa)
     
    0.919
nuoC
NADH (or F420H2) dehydrogenase, subunit C; NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (209 aa)
     
    0.917
Slit_0167
Hypothetical protein (384 aa)
     
 
    0.911
Slit_1437
Squalene synthase HpnC (271 aa)
     
 
    0.911
Slit_1436
Squalene synthase HpnD (277 aa)
     
 
    0.911
Slit_2237
NmrA family protein (282 aa)
   
 
    0.910
nuoD
NADH dehydrogenase I, D subunit; NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (417 aa)
     
 
    0.910
Slit_0034
AmpG-related permease (419 aa)
   
   
  0.892
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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