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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
aroKShikimate kinase; Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate; Belongs to the shikimate kinase family. (437 aa)    
Predicted Functional Partners:
aroB
3-dehydroquinate synthase; Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
 
 0.999
APA98492.1
Belongs to the dehydroquinate synthase family; KEGG: ppu:PP_5078 3-dehydroquinate synthase.
 
 0.996
aroE
Shikimate dehydrogenase; The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis; In the N-terminal sectio; belongs to the dehydroquinate synthase family; In the 2nd sectio; belongs to the EPSP synthase family; In the 3rd sectio; belongs to the shikimate kinase family; In the 4th sectio; belongs to the type-I 3- dehydroquinase family; In the C-terminal sectio; belongs to the shikimate dehydrogenase family; KEGG: mtu:Rv2552c shikimate dehydrogenase.
 
 
 0.990
aroA
3-phosphoshikimate 1-carboxyvinyltransferase; 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.
 
 
 0.987
aroC
Chorismate synthase; 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.
 
  
 0.987
aroQ
3-dehydroquinate dehydratase; Catalyzes a trans-dehydration via an enolate intermediate. Belongs to the type-II 3-dehydroquinase family.
 
  
 0.968
APB01828.1
3-deoxy-7-phosphoheptulonate synthase; Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino- heptulosonate-7-phosphate (DAHP).
  
 
 0.964
APA99981.1
C7-cyclitol synthase using sedo-heptulose 7-phosphate, but not ido-heptulose 7-phosphate and 3-deoxy-arabino- heptulosonate 7-phosphate, as a substrate. Involved in the biosynthesis of the acarviose moiety of the alpha-glucosidase inhibitor acarbose. Belongs to the dehydroquinate synthase family; KEGG: mmi:MMAR_0578 3-dehydroquinate synthase.
  
 0.941
aroF
3-deoxy-7-phosphoheptulonate synthase; Catalyzes an aldol-like condensation reaction between phosphoenolpyruvate (PEP) and D-erythrose 4-phosphate (E4P) to generate 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAH7P) and inorganic phosphate; Belongs to the class-II DAHP synthase family; KEGG: mtu:Rv2178c 3-deoxy-7-phosphoheptulonate synthase.
    
 0.935
APA94940.1
Prephenate dehydrogenase; Catalyzes the NAD(+)-dependent conversion of prephenate to p-hydroxyphenylpyruvate, with the elimination of carbon dioxide. Is a key regulatory enzyme in tyrosine biosynthesis. Displays no chorismate mutase (CM) activity, in contrast to TyrA from E. coli and some other bacteria, that are bifunctional and possess a CM domain; Contains 1 prephenate/arogenate dehydrogenase domain; KEGG: pdx:Psed_0331 prephenate dehydrogenase.
 
  
 0.769
Your Current Organism:
Nocardia seriolae
NCBI taxonomy Id: 37332
Other names: ATCC 43993, CCUG 46828, CIP 104778, DSM 44129, IFO 15557, JCM 3360, N. seriolae, NBRC 15557
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