STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
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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[Homology]
Score
hisBPFAM: imidazoleglycerol-phosphate dehydratase; KEGG: gme:Gmet_0386 imidazoleglycerol-phosphate dehydratase. (195 aa)    
Predicted Functional Partners:
hisC-2
TIGRFAM: histidinol-phosphate aminotransferase; PFAM: aminotransferase, class I and II; KEGG: gme:Gmet_0385 histidinol-phosphate aminotransferase; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.
 
 0.999
hisD
Histidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine.
  
 0.999
hisF
Imidazole glycerol phosphate synthase subunit hisF; 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.
 
 
 0.999
hisH
Imidazole glycerol phosphate synthase subunit hisH; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF.
 
 
 0.999
hisC
TIGRFAM: histidinol-phosphate aminotransferase; PFAM: aminotransferase, class I and II; KEGG: reu:Reut_A2574 histidinol-phosphate aminotransferase; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.
 
 0.996
hisI
phosphoribosyl-AMP cyclohydrolase; Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
 
  
 0.990
hisA
1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; KEGG: gsu:GSU3096 phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; TIGRFAM: phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; PFAM: histidine biosynthesis.
 
  
 0.990
hisG-2
ATP phosphoribosyltransferase (homohexameric); 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. Belongs to the ATP phosphoribosyltransferase family. Short subfamily.
 
  
 0.987
hisE
PFAM: MazG nucleotide pyrophosphohydrolase; phosphoribosyl-ATP pyrophosphohydrolase; KEGG: gme:Gmet_0390 phosphoribosyl-ATP pyrophosphohydrolase.
 
  
 0.986
hisG
ATP phosphoribosyltransferase (homohexameric); 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. Belongs to the ATP phosphoribosyltransferase family. Long subfamily.
 
  
 0.929
Your Current Organism:
Pelobacter propionicus
NCBI taxonomy Id: 338966
Other names: P. propionicus DSM 2379, Pelobacter propionicus DSM 2379, Pelobacter propionicus str. DSM 2379, Pelobacter propionicus strain DSM 2379
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.