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hisB protein (Sideroxydans lithotrophicus) - STRING interaction network
"hisB" - Imidazoleglycerol-phosphate dehydratase in Sideroxydans lithotrophicus
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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
hisBImidazoleglycerol-phosphate dehydratase (195 aa)    
Predicted Functional Partners:
hisH
Imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit provides the glutamine amidotransferase activity that produces the ammonia necessary to HisF for the synthesis of IGP and AICAR (239 aa)
 
 
  0.999
hisF
Imidazoleglycerol phosphate synthase, cyclase subunit; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit (252 aa)
 
 
  0.999
Slit_0624
Histidinol-phosphate aminotransferase (364 aa)
 
  0.999
hisA
Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase (253 aa)
   
  0.997
hisD
Histidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine (432 aa)
   
  0.993
Slit_2064
Histidinol-phosphate aminotransferase (373 aa)
 
  0.992
hisI
phosphoribosyl-AMP cyclohydrolase; Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP (129 aa)
 
   
  0.980
hisG
ATP phosphoribosyltransferase; Catalyzes the condensation of ATP and 5-phosphoribose 1- diphosphate to form N’-(5’-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity (212 aa)
 
   
  0.965
hisE
phosphoribosyl-ATP diphosphatase (105 aa)
 
   
  0.960
guaA
GMP synthase, large subunit; Catalyzes the synthesis of GMP from XMP (526 aa)
   
   
  0.798
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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