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queH protein (Alcaligenes faecalis) - STRING interaction network
"queH" - Epoxyqueuosine reductase QueH in Alcaligenes faecalis
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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queHEpoxyqueuosine reductase QueH; Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr) (232 aa)    
Predicted Functional Partners:
rnhB
Ribonuclease HII; Endonuclease that specifically degrades the RNA of RNA- DNA hybrids (201 aa)
            0.763
glnE
Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory regi [...] (918 aa)
              0.665
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) (275 aa)
           
  0.613
queA
S-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) (354 aa)
 
     
  0.562
JT27_17500
Uncharacterized protein; Derived by automated computational analysis using gene prediction method- Protein Homology (1201 aa)
              0.449
Your Current Organism:
Alcaligenes faecalis
NCBI taxonomy Id: 511
Other names: A. faecalis, ATCC 8750, Alcaligenes faecalis, Alcaligenes sp. BP11, CIP 55.84, CIP 60.80, DSM 30030, IAM 12369, IFO 13111, JCM 20522, JCM 20663, NBRC 13111, NCAIM B.01104, NCIMB 8156, NCTC 11953
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