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
Your Input:
Neighborhood
Gene fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
aroBPutative alternative 3-dehydroquinate synthase; Catalyzes the oxidative deamination and cyclization of 2- amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3- dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis; Belongs to the archaeal-type DHQ synthase family. (392 aa)    
Predicted Functional Partners:
aroA-2
Putative phospho-2-dehydro-3-deoxyheptonate aldolase; 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.
 
 
 0.996
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. Belongs to the type-I 3-dehydroquinase family.
 
  
 0.955
AGB15337.1
DhnA-type fructose-1,6-bisphosphate aldolase-like enzyme; PFAM: DeoC/LacD family aldolase.
 
  
 0.889
AGB17275.1
PFAM: Prephenate dehydratase; ACT domain.
 
  
 0.831
AGB16189.1
PFAM: Chorismate mutase type II; TIGRFAM: chorismate mutase, archaeal type.
  
  
 0.822
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.
 
   
 0.757
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.
 
   
 0.746
aroE
Shikimate 5-dehydrogenase; 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).
 
   
 0.736
aroK
PFAM: GHMP kinases N terminal domain; TIGRFAM: shikimate kinase.
 
   
 0.658
trpC
PFAM: Indole-3-glycerol phosphate synthase; Belongs to the TrpC family.
     
 0.610
Your Current Organism:
Halovivax ruber
NCBI taxonomy Id: 797302
Other names: H. ruber XH-70, Halovivax ruber JCM 13892, Halovivax ruber XH-70, Halovivax ruber str. XH-70, Halovivax ruber strain XH-70
Server load: low (22%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.