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queA protein (Nitrosomonas eutropha) - STRING interaction network
"queA" - S-adenosylmethionine:tRNA ribosyltransferase-isomerase in Nitrosomonas eutropha
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
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some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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queAS-adenosylmethionine-tRNA ribosyltransferase-isomerase; Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA) (346 aa)    
Predicted Functional Partners:
tgt
Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1’ of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1’ of the ribose to form th [...] (361 aa)
 
  0.999
Neut_1432
TIGRFAM- preprotein translocase, YajC subunit; PFAM- YajC family protein; KEGG- neu-NE1142 putative preprotein translocase YajC subunit (154 aa)
       
  0.937
secF
Protein-export membrane protein SecF; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA (310 aa)
     
  0.931
secD
Protein translocase subunit SecD; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA (615 aa)
   
  0.930
ruvB
Holliday junction ATP-dependent DNA helicase RuvB; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing (346 aa)
 
 
  0.758
queF
NADPH-dependent 7-cyano-7-deazaguanine reductase; Catalyzes the NADPH-dependent reduction of 7-cyano-7- deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1); Belongs to the GTP cyclohydrolase I family. QueF type 1 subfamily (139 aa)
 
   
  0.698
queC
7-cyano-7-deazaguanine synthase; Catalyzes the ATP-dependent conversion of 7-carboxy-7- deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)); Belongs to the QueC family (226 aa)
 
   
  0.651
Neut_1286
Uncharacterized protein; PFAM- 6-pyruvoyl tetrahydropterin synthase and hypothetical protein; KEGG- neu-NE1517 6-pyruvoyl tetrahydropterin synthase (160 aa)
 
   
  0.620
ruvA
Holliday junction ATP-dependent DNA helicase RuvA; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB (194 aa)
 
   
  0.608
queE
7-carboxy-7-deazaguanine synthase; Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7- carboxy-7-deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds (211 aa)
   
   
  0.607
Your Current Organism:
Nitrosomonas eutropha
NCBI taxonomy Id: 335283
Other names: N. eutropha C91, Nitrosomonas eutropha, Nitrosomonas eutropha C91, Nitrosomonas eutropha str. C91, Nitrosomonas eutropha strain C91
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