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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Textmining
[Homology]
Score
hisCHistidinol-phosphate aminotransferase; Catalyzes the formation of L-histidinol phosphate from imidazole-acetol phosphate and glutamate in histidine biosynthesis; 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. (368 aa)    
Predicted Functional Partners:
hisB
Imidazoleglycerol-phosphate dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.999
ALV26932.1
Cyclohexadienyl dehydrogenase; Dual function enzyme catalyzes the formation of 4-hydroxyphenylpyruvate from prephenate and the formation of tyrosine from arogenate; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.998
hisD
Histidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine.
  
 0.995
ALV26934.1
Chorismate mutase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.972
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.
 
  
 0.966
ALV25919.1
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.
 
  
 0.957
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.
 
  
 0.950
hisI
phosphoribosyl-AMP cyclohydrolase; Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
 
  
 0.946
hisA
Catalyzes the formation of 5-(5-phospho-1-deoxyribulos-1-ylamino)methylideneamino-l- (5-hosphoribosyl)imidazole-4-carboxamide from 1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino] imidazole-4-carboxamide; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.939
ALV26564.1
Prephenate dehydratase; Catalyzes the formation of phenylpyruvate from prephenate in phenylalanine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.935
Your Current Organism:
Pannonibacter phragmitetus
NCBI taxonomy Id: 121719
Other names: Achromobacter group B, Achromobacter group E, Achromobacter sp. LMG 5410, Achromobacter sp. LMG 5411, Achromobacter sp. LMG 5430, Achromobacter sp. LMG 5431, DSM 14782, LMG 22736, LMG:22736, NCAIM B02025, NCTC 13350, P. phragmitetus, Pannonibacter phragmitetus Borsodi et al. 2003, alpha proteobacterium C6-19, alpha proteobacterium C6/17, alpha proteobacterium C6/8, strain C6/19
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