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
hisHImidazole 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. (193 aa)    
Predicted Functional Partners:
hisI
phosphoribosyl-ATP pyrophosphatase; Catalyzes the formation of 1-(5-phosphoribosyl)-AMP from 1-(5-phosphoribosyl)-ATP and the subsequent formation of 1-(5-phosphoribosyl)-5-((5- phosphoribosylamino)methylideneamino)imidazole-4- carboxamide from 1-(5-phosphoribosyl)-AMP in histidine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology; In the N-terminal section; belongs to the PRA-CH family.
  
 0.999
hisF
Imidazole glycerol 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.
 0.999
hisA
1-(5-phosphoribosyl)-5-((5- phosphoribosylamino)methylideneamino)imidazole-4- carboxamide isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.999
hisB
Imidazoleglycerol-phosphate dehydratase; Catalyzes the formation of 3-(imidazol-4-yl)-2-oxopropyl phosphate from D-ethythro-1-(imidazol-4-yl)glycerol 3-phosphate and histidinol from histidinol phosphate; Derived by automated computational analysis using gene prediction method: Protein Homology; In the C-terminal section; belongs to the imidazoleglycerol-phosphate dehydratase family.
 
 0.999
hisD
Histidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine.
  
 0.994
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. Long subfamily.
 
  
 0.986
hisC
Histidinol phosphate aminotransferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.
 
  
 0.972
purH
Phosphoribosylaminoimidazolecarboxamide formyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.844
AMC10472.1
Adenylosuccinate lyase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.
    
 0.813
AMC10309.1
L-threonine O-3-phosphate decarboxylase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.804
Your Current Organism:
Lutibacter profundi
NCBI taxonomy Id: 1622118
Other names: DSM 100437, JCM 30586, L. profundi, Lutibacter profundi Le Moine Bauer et al. 2016, Lutibacter sp. LP1, strain LP1
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