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Queuine tRNA-ribosyltransferase (Francisella tularensis subsp. holarctica OSU18)

Protein
Dates
  • Create:
    2017-04-15
  • Modify:
    2025-01-19
Description
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 the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).

1 Names and Identifiers

1.1 Synonyms

  • Queuine tRNA-ribosyltransferase
  • EC 2.4.2.29
  • Guanine insertion enzyme
  • tRNA-guanine transglycosylase

1.2 Other Identifiers

1.2.1 RefSeq Accession

1.2.2 UniProt ID

1.2.3 Enzyme Commission (EC) Number

1.2.4 InterPro Protein

2 Sequence

>sp|Q0BMC7|TGT_FRATO Queuine tRNA-ribosyltransferase (Run BLAST)

MTVMKFDLIKKEGKARRGKITFPRGDIQTPAFMPVGTYGAVKSLSPVELKEMGAEIILGNTFHLWLRPGTEIIKKHGSLHGFNGWDKPILTDSGGFQVFSLGKMRKLTEEGVTFKSPVNSSKVFLSPEISMQVQRDLGSDIVMCFDECTPYPATEKEAKESMELSMRWAKRSKEAHGDNPSALFGIIQGGMYEHLRDESLAKLKEIDFDGFAIGGLSVGEPKEDMIRILDHTAHQMPEDKPRYLMGVGTPKDLVEAVYRGVDMFDCVMPSRNARNGHIFTSEGVIKIRNSKYKDDTSPLDPNCDCYTCKNFTKSYLHHLDKTKEILGSRLNTIHNLTFYQNLMKSIRKALDEGRFSEFRKEFLASYK

3 Domains

3.1 CDD Domains

3.2 InterPro Domains

4 Biochemical Reactions

5 Literature

5.1 Consolidated References

6 Patents

7 Information Sources

  1. NCBI Protein
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    https://www.ncbi.nlm.nih.gov/home/about/policies/
  2. PubChem
  3. InterPro
    LICENSE
    All of the InterPro, Pfam, PRINTS and SFLD downloadable data provided on the InterPro website is freely available under CC0 1.0 Universal (CC0 1.0) Public Domain Dedication.
    https://www.ebi.ac.uk/interpro/about/license/
  4. NCBI Conserved Domains (CDD)
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    https://www.ncbi.nlm.nih.gov/home/about/policies/
  5. UniProt
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    https://www.uniprot.org/help/license
  6. Rhea - annotated reactions database
    LICENSE
    Rhea has chosen to apply the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/). This means that you are free to copy, distribute, display and make commercial use of the database in all legislations, provided you credit (cite) Rhea.
    https://www.rhea-db.org/help/license-disclaimer
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