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:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
hisEBifunctional phosphoribosyl-AMP cyclohydrolase/phosphoribosyl-ATP diphosphatase; 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. (203 aa)    
Predicted Functional Partners:
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.
 
 
 0.999
hisD
Histidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine.
  
 0.999
hisC
Histidinol-phosphate transaminase; 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.
 
  
 0.999
hisB
Bifunctional imidazole glycerol-phosphate dehydratase/histidinol phosphatase; 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; Belongs to the imidazoleglycerol-phosphate dehydratase family. In the N-terminal section; belongs to the histidinol- phosphatase family.
  
 0.999
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.
  
 0.999
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
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.
  
 0.999
AOE38789.1
Acid phosphatase AphA; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.942
serB
Phosphoserine phosphatase SerB; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.942
AOE40724.1
Hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.942
Your Current Organism:
Pantoea agglomerans
NCBI taxonomy Id: 549
Other names: ATCC 27155, Bacillus milletiae, Bacterium herbicola, CCUG 539, CFBP 3845, CIP 57.51, DSM 3493, Enterobacter agglomerans, Erwinia herbicola, Erwinia milletiae, ICMP 12534, ICPB 3435, NBRC 102470, NCTC 9381, P. agglomerans, Pantoea herbicola, Pantoea sp. SL1_M5, Pseudomonas herbicola, bacterium G33-1
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