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
STM3859Similar to E. coli dehydroshikimate reductase (AAC76306.1); Blastp hit to AAC76306.1 (272 aa), 26% identity in aa 20 - 258; quinate 5-dehydrogenase. (272 aa)    
Predicted Functional Partners:
aroL
Shikimate kinase II; Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
 
 
 0.977
aroD
3-dehydroquinate dehydratase; Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis- dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. The reaction involves the formation of an imine intermediate between the keto group of 3-dehydroquinate and the epsylon-amino group of a lys-170 at the active site. Belongs to the type-I 3-dehydroquinase family.
  
 0.967
aroK
Shikimate kinase I; Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate; Belongs to the shikimate kinase family.
 
 
 0.966
ydiB
Putative shikimate 5-dehydrogenase; The actual biological function of YdiB remains unclear, nor is it known whether 3-dehydroshikimate or quinate represents the natural substrate. Catalyzes the reversible NAD-dependent reduction of both 3-dehydroshikimate (DHSA) and 3-dehydroquinate to yield shikimate (SA) and quinate, respectively. It can use both NAD or NADP for catalysis, however it has higher catalytic efficiency with NAD.
 
  
0.945
aroE
Dehydroshikimate reductase; Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
  
  
0.926
aroA
3-enolpyruvylshikimate-5-phosphate synthetase; Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
 
  
 0.896
yjbG
Putative periplasmic protein; Similar to E. coli orf, hypothetical protein (AAC76998.1); Blastp hit to AAC76998.1 (245 aa), 74% identity in aa 1 - 245.
  
  
 0.893
menF
Isochorismate synthase; Catalyzes the conversion of chorismate to isochorismate.
  
  
 0.878
entC
Similar to E. coli isochorismate hydroxymutase 2, enterochelin biosynthesis (AAC73694.1); Blastp hit to AAC73694.1 (391 aa), 84% identity in aa 1 - 391.
     
 0.828
yrdB
Putative periplasmic protein; Similar to E. coli orf, hypothetical protein (AAC76305.1); Blastp hit to AAC76305.1 (85 aa), 71% identity in aa 1 - 84.
  
  
 0.770
Your Current Organism:
Salmonella enterica Typhimurium
NCBI taxonomy Id: 99287
Other names: S. enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium LT2, Salmonella enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2-LTL2, Salmonella typhimurium LT2
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.