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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
hisJHistidinol phosphate phosphatase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the PHP hydrolase family. HisK subfamily. (268 aa)    
Predicted Functional Partners:
hisC
Histidinol-phosphate aminotransferase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.
 
 
 0.981
hisD
Histidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine.
 
 
 0.977
hisB
Imidazoleglycerol-phosphate dehydratase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme.
 
  
 0.906
hisI
phosphoribosyl-AMP cyclohydrolase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; In the C-terminal section; belongs to the PRA-PH family.
  
  
 0.817
ezrA
Negative regulator of FtsZ ring formation; Negative regulator of FtsZ ring formation; modulates the frequency and position of FtsZ ring formation. Inhibits FtsZ ring formation at polar sites. Interacts either with FtsZ or with one of its binding partners to promote depolymerization.
  
    0.691
hisF
Imidazole glycerol phosphate synthase 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 (By similarity).
 
  
 0.654
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.
 
  
 0.632
hisA
Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme.
 
  
 0.562
pabA
4-amino-4-deoxychorismate synthase; Part of a heterodimeric complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p- aminobenzoate (PABA) and tetrahydrofolate. In the first step, a glutamine amidotransferase (PabA) generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by aminodeoxychorismate synthase (PabB) to produce ADC. PabA converts glutamine into glutamate only in the presence of stoichiometric amounts of PabB. Also involved in the biosynthesis of anthranilate.
   
  
 0.532
gltA
Glutamate synthase (large subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the glutamate synthase family.
  
  
 0.474
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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