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Information on EC 2.4.2.29 - tRNA-guanosine34 preQ1 transglycosylase and Organism(s) Methanosarcina acetivorans and UniProt Accession Q8THU2

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.29 tRNA-guanosine34 preQ1 transglycosylase
IUBMB Comments
Certain prokaryotic and eukaryotic tRNAs contain the modified base queuine at position 34. In eubacteria, which produce queuine de novo, the enzyme catalyses the exchange of guanine with the queuine precursor preQ1, which is ultimately modified to queuosine . The enzyme can also use an earlier intermediate, preQ0, to replace guanine in unmodified tRNATyr and tRNAAsn . This enzyme acts after EC 1.7.1.13, preQ1 synthase, in the queuine-biosynthesis pathway. cf. EC 2.4.2.64, tRNA-guanosine34 queuine transglycosylase.
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This record set is specific for:
Methanosarcina acetivorans
UNIPROT: Q8THU2
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The taxonomic range for the selected organisms is: Methanosarcina acetivorans
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
trna-guanine transglycosylase, arctgt, qtrt1, trna guanine transglycosylase, trna transglycosylase, guanine insertion enzyme, queuine trna-ribosyltransferase, trna-guanine 34 transglycosylase, q-insertase, queuine trna ribosyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
guanine insertion enzyme
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guanine, queuine-tRNA transglycosylase
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Q-insertase
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queuine insertase
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queuine tRNA ribosyltransferase
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queuine tRNA-ribosyltransferase
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ribosyltransferase, queuine transfer ribonucleate
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TGT
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transfer ribonucleate glycosyltransferase
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tRNA guanine transglycosidase
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tRNA guanine transglycosylase
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tRNA transglycosylase
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tRNA-guanine transglycosylase
virulence-associated protein VACC
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pentosyl group transfer
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-
PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
tRNA-guanosine34:7-aminomethyl-7-deazaguanine tRNA-D-ribosyltransferase
Certain prokaryotic and eukaryotic tRNAs contain the modified base queuine at position 34. In eubacteria, which produce queuine de novo, the enzyme catalyses the exchange of guanine with the queuine precursor preQ1, which is ultimately modified to queuosine [5]. The enzyme can also use an earlier intermediate, preQ0, to replace guanine in unmodified tRNATyr and tRNAAsn [1]. This enzyme acts after EC 1.7.1.13, preQ1 synthase, in the queuine-biosynthesis pathway. cf. EC 2.4.2.64, tRNA-guanosine34 queuine transglycosylase.
CAS REGISTRY NUMBER
COMMENTARY hide
72162-89-1
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
Q8THU2; Q8TUE6
optimal concentration : 10 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
Q8THU2; Q8TUE6
pH 7.0: about 50% of maximal activity, pH 9.0: about 50% oif maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
Q8THU2; Q8TUE6
in the first step of archaeosine biosynthesis, archaeosine tRNAguanine transglycosylase catalyzes the base exchange reaction from guanine to 7-cyano-7-deazaguanine
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
150000
Q8THU2; Q8TUE6
gel filtration
19000
Q8THU2; Q8TUE6
2 * 19000 + 2 * 54000, archaeosine tRNAguanine transglycosylase is classified into full-size or split types. Although the full-size type forms a homodimeric structure, the split type forms a heterotetrameric structure, consisting of two kinds of peptide. Interaction between the two subunits may contribute to the conformational stability of split ArcTGT
54000
Q8THU2; Q8TUE6
2 * 19000 + 2 * 54000, archaeosine tRNAguanine transglycosylase is classified into full-size or split types. Although the full-size type forms a homodimeric structure, the split type forms a heterotetrameric structure, consisting of two kinds of peptide. Interaction between the two subunits may contribute to the conformational stability of split ArcTGT
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterotetramer
Q8THU2; Q8TUE6
2 * 19000 + 2 * 54000, archaeosine tRNAguanine transglycosylase is classified into full-size or split types. Although the full-size type forms a homodimeric structure, the split type forms a heterotetrameric structure, consisting of two kinds of peptide. Interaction between the two subunits may contribute to the conformational stability of split ArcTGT
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
Q8THU2; Q8TUE6
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nomura, Y.; Onda, Y.; Ohno, S.; Taniguchi, H.; Ando, K.; Oka, N.; Nishikawa, K.; Yokogawa, T.
Purification and comparison of native and recombinant tRNA-guanine transglycosylases from Methanosarcina acetivorans
Protein Expr. Purif.
88
13-19
2013
Methanosarcina acetivorans (Q8THU2 and Q8TUE6), Methanosarcina acetivorans, Methanosarcina acetivorans DSM 2834 (Q8THU2 and Q8TUE6)
Manually annotated by BRENDA team