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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
MJ_0612Chorismate mutase/prephenate dehydratase (tyrA); Similar to SP:P07023 PID:457110 GB:U00096 PID:1788952 percent identity: 33.46; identified by sequence similarity; putative; In the N-terminal section; belongs to the prephenate/arogenate dehydrogenase family. (446 aa)    
Predicted Functional Partners:
pheA
Chorismate mutase/prephenate dehydratase (pheA); Similar to SP:P43909 PID:683585 percent identity: 38.59; identified by sequence similarity; putative.
 
 0.998
aroQ
Chorismate mutase/prephenate dehydratase (pheA); Catalyzes the conversion of chorismate into prephenate via a Claisen rearrangement.
 
 
 0.983
MJ_0001
Aspartate aminotransferase (aspB1); Similar to PID:1146246 SP:P53001 GB:AL009126 percent identity: 44.38; identified by sequence similarity; putative; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.
    
 0.923
hisC
Histidinol-phosphate aminotransferase (hisC); Similar to SP:P06986 GB:U02071 GB:X03416 PID:41695 PID:41710 percent identity: 29.00; identified by sequence similarity; putative.
    
 0.918
aroC
Chorismate synthase (aroC); Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
 
  
 0.853
aroA-2
3-phosphoshikimate-1-carboxyvinyltransferase (aroA); 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.
 
  
 0.824
aroE
Shikimate 5-dehydrogenase (aroE); 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).
     
 0.731
aroD
3-dehydroquinate dehydratase (aroD); 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. Belongs to the type-I 3-dehydroquinase family.
     
 0.731
aroK
Conserved hypothetical protein; Similar to GB:AE000666 percent identity: 44.16; identified by sequence similarity; putative.
 
     0.726
aroA
Conserved hypothetical protein; Catalyzes a transaldol reaction between 6-deoxy-5- ketofructose 1-phosphate (DKFP) and L-aspartate semialdehyde (ASA) with an elimination of hydroxypyruvaldehyde phosphate to yield 2-amino-3,7- dideoxy-D-threo-hept-6-ulosonate (ADH). Plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids. Can also catalyze the cleavage of fructose-1,6- bisphosphate (FBP) to glyceraldehyde-3-phosphate (GAP) and dihydroxyacetone phosphate (DHAP).
       0.685
Your Current Organism:
Methanocaldococcus jannaschii
NCBI taxonomy Id: 243232
Other names: M. jannaschii DSM 2661, Methanocaldococcus jannaschii DSM 2661, Methanocaldococcus jannaschii str. DSM 2661, Methanococcus jannaschii DSM 2661
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