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
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
hisCKEGG: asu:Asuc_0923 histidinol-phosphate aminotransferase; TIGRFAM: histidinol-phosphate aminotransferase; PFAM: aminotransferase class I and II; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. (366 aa)    
Predicted Functional Partners:
hisB
KEGG: gme:Gmet_0386 imidazoleglycerol-phosphate dehydratase; PFAM: imidazoleglycerol-phosphate dehydratase.
 
 0.999
Bsel_2120
KEGG: geo:Geob_2360 prephenate dehydrogenase; PFAM: Prephenate dehydrogenase; NADP oxidoreductase coenzyme F420-dependent; amino acid-binding ACT domain protein; 6-phosphogluconate dehydrogenase NAD-binding.
  
 
 0.995
hisD
Histidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine.
  
 0.993
hisI
phosphoribosyl-ATP diphosphatase; KEGG: ppr:PBPRA1085 bifunctional phosphoribosyl-AMP cyclohydrolase/phosphoribosyl-ATP pyrophosphatase protein; TIGRFAM: phosphoribosyl-ATP diphosphatase; PFAM: phosphoribosyl-AMP cyclohydrolase; phosphoribosyl-ATP pyrophosphohydrolase; In the N-terminal section; belongs to the PRA-CH family.
 
  
 0.990
Bsel_1325
KEGG: sun:SUN_0354 PHP family histidinol phosphatase/hydrolase; TIGRFAM: histidinol phosphate phosphatase HisJ family; PFAM: PHP domain protein; Belongs to the PHP hydrolase family. HisK subfamily.
 
 
 0.958
hisH
Imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; 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.
 
  
 0.945
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.
 
  
 0.945
pheA
KEGG: afw:Anae109_2039 prephenate dehydratase; PFAM: prephenate dehydratase; amino acid-binding ACT domain protein.
  
 
 0.938
hisA
TIGRFAM: phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; KEGG: cff:CFF8240_1351 1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; PFAM: histidine biosynthesis protein.
 
  
 0.936
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. Belongs to the ATP phosphoribosyltransferase family. Short subfamily.
 
  
 0.935
Your Current Organism:
Bacillus selenitireducens
NCBI taxonomy Id: 439292
Other names: Bacillus selenitireducens MLS10, [. selenitireducens MLS10, [Bacillus] selenitireducens MLS10
Server load: low (12%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.