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
Databases
Textmining
[Homology]
Score
AMG70527.1Aminotransferase class I; Derived by automated computational analysis using gene prediction method: Protein Homology. (389 aa)    
Predicted Functional Partners:
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; In the N-terminal section; belongs to the histidinol- phosphatase family.
 
 0.998
tyrA
Bifunctional chorismate mutase/prephenate dehydrogenase; Catalyzes the formation of prephenate from chorismate and the formation of 4-hydroxyphenylpyruvate from prephenate in tyrosine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.982
hisI
Bifunctional 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.
 
  
 0.980
pheA
Bifunctional chorismate mutase/prephenate dehydratase; Catalyzing the formation of prephenate from chorismate and the formation of phenylpyruvate from prephenate in phenylalanine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.952
hisD
Histidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine.
  
 0.943
hisC
Histidinol-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.
  
  
 
0.920
AMG69374.1
Aromatic amino acid aminotransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.909
AMG71928.1
Catalyzes the formation of L-glutamate and an aromatic oxo acid from an aromatic amino acid and 2-oxoglutarate; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.909
AMG69442.1
GNAT family acetyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
  0.900
dadA
D-amino acid dehydrogenase small subunit; Oxidative deamination of D-amino acids.
   
 
 0.900
Your Current Organism:
Morganella morganii
NCBI taxonomy Id: 582
Other names: ATCC 25830, ATCC 8076H, Bacillus morgani, CCUG 6328, CIP 103763, CIP A231, DSM 30164, IFO 3848, LMG 7874, LMG:7874, M. morganii, NBRC 3848, NCCB 73065, NCIB 235, NCIB:235, NCTC 235, Organism N 1, Proteus morganii, Salmonella morgani
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