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aroQ protein (Desulfovibrio vulgaris Hildenborough) - STRING interaction network
"aroQ" - 3-dehydroquinate dehydratase in Desulfovibrio vulgaris Hildenborough
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second shell of interactors
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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aroQ3-dehydroquinate dehydratase; Catalyzes a trans-dehydration via an enolate intermediate; Belongs to the type-II 3-dehydroquinase family (155 aa)    
Predicted Functional Partners:
aroE
Shikimate dehydrogenase (NADP(+)); 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) (301 aa)
 
  0.989
DVU_0461
Predicted 3-dehydroquinate synthase; Identified by similarity to OMNI-NTL01AA01322 (323 aa)
         
  0.900
aroK-1
Shikimate kinase; Identified by similarity to SP-P10880; match to protein family HMM PF01202 (175 aa)
   
  0.859
DVU_0296
Peptidase, M24 family; Identified by match to protein family HMM PF00557 (356 aa)
            0.842
efp
Elongation factor P; Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase (185 aa)
         
  0.800
DVU_2339
annotation not available (283 aa)
          0.770
DVU_0462
Chorismate mutase/prephenate dehydratase; Identified by similarity to SP-P07022; match to protein family HMM PF00800; match to protein family HMM PF01817; match to protein family HMM PF01842; match to protein family HMM TIGR01807 (391 aa)
         
  0.755
engB
Probable GTP-binding protein EngB; Necessary for normal cell division and for the maintenance of normal septation (216 aa)
              0.691
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 (354 aa)
 
     
  0.682
ilvE
Branched-chain-amino-acid aminotransferase; Acts on leucine, isoleucine and valine; Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family (309 aa)
 
   
  0.682
Your Current Organism:
Desulfovibrio vulgaris Hildenborough
NCBI taxonomy Id: 882
Other names: D. vulgaris str. Hildenborough, Desulfovibrio vulgaris (STRAIN HILDENBOROUGH), Desulfovibrio vulgaris ATCC 29579, Desulfovibrio vulgaris Hildenborough, Desulfovibrio vulgaris str. Hildenborough, Desulfovibrio vulgaris subsp. vulgaris (strain Hildenborough), Desulfovibrio vulgaris subsp. vulgaris ATCC 29579, Desulfovibrio vulgaris subsp. vulgaris str. Hildenborough
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