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
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[Homology]
Score
hisZhistidyl-tRNA synthetase-related protein; Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine (By similarity). (275 aa)    
Predicted Functional Partners:
hisS
histidyl-tRNA synthetase; Similar to GB:AL009126 percent identity: 66.83; identified by sequence similarity; putative.
     
 0.992
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 (By similarity); Belongs to the ATP phosphoribosyltransferase family. Short subfamily.
 
 0.991
hisI
phosphoribosyl-AMP cyclohydrolase / phosphoribosyl-ATP pyrophosphohydrolase; Similar to GB:AE000657 percent identity: 70.41; identified by sequence similarity; putative; In the C-terminal section; belongs to the PRA-PH family.
 
 
 0.977
hisC
Histidinol-phosphate aminotransferase; Similar to GB:AE000657 percent identity: 59.04; identified by sequence similarity; putative; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.
 
  
 0.890
hisD
Histidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine.
 
   
 0.873
hisB
Imidazoleglycerol-phosphate dehydratase; Similar to SP:P56090 PID:2226092 percent identity: 56.08; identified by sequence similarity; putative.
 
  
 0.868
hisA
Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; Similar to GB:M90760 SP:Q02131 PID:149382 percent identity: 56.30; identified by sequence similarity; putative; Belongs to the HisA/HisF family.
 
   
 0.865
hisF
Cyclase; 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.
 
   
 0.850
hisH
Amidotransferase; 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.
  
  
 0.831
aspS
aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
  
  
 0.759
Your Current Organism:
Thermotoga maritima
NCBI taxonomy Id: 243274
Other names: T. maritima MSB8, Thermotoga maritima DSM 3109, Thermotoga maritima MSB8, Thermotoga maritima str. MSB8, Thermotoga maritima strain MSB8
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.