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Queuine tRNA-ribosyltransferase (EC 2.4.2.29) (Guanine insertion enzyme) (tRNA-guanine transglycosylase)

 TGT_ZYMMO               Reviewed;         386 AA.
P28720; Q5NQL7; Q60247; Q9F5L7;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
20-DEC-2017, entry version 155.
RecName: Full=Queuine tRNA-ribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00168};
EC=2.4.2.29 {ECO:0000255|HAMAP-Rule:MF_00168};
AltName: Full=Guanine insertion enzyme {ECO:0000255|HAMAP-Rule:MF_00168};
AltName: Full=tRNA-guanine transglycosylase {ECO:0000255|HAMAP-Rule:MF_00168};
Name=tgt {ECO:0000255|HAMAP-Rule:MF_00168}; OrderedLocusNames=ZMO0363;
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
Sphingomonadaceae; Zymomonas.
NCBI_TaxID=264203;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-7, FUNCTION,
CATALYTIC ACTIVITY, PATHWAY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=7665516; DOI=10.1128/jb.177.18.5284-5288.1995;
Reuter K.K.H., Ficner R.;
"Sequence analysis and overexpression of the Zymomonas mobilis tgt
gene encoding tRNA-guanine transglycosylase: purification and
biochemical characterization of the enzyme.";
J. Bacteriol. 177:5284-5288(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 31821 / ZM4 / CP4;
Ahn J.Y., Kang H.S.;
"Sequence analysis of 44B6 fosmid clone of Zymomonas mobilis ZM4.";
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 31821 / ZM4 / CP4;
PubMed=15592456; DOI=10.1038/nbt1045;
Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J.,
Hong J.H., Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M.,
Lee J.-S., Jin S.-J., Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y.,
Kang H.L., Lee S.Y., Lee K.J., Kang H.S.;
"The genome sequence of the ethanologenic bacterium Zymomonas mobilis
ZM4.";
Nat. Biotechnol. 23:63-68(2005).
[4]
PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 31821 / ZM4 / CP4;
PubMed=1526462; DOI=10.1016/0378-1097(92)90450-3;
Shark K.B., Conway T.;
"Cloning and molecular characterization of the DNA ligase gene (lig)
from Zymomonas mobilis.";
FEMS Microbiol. Lett. 75:19-26(1992).
[5]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-386 IN COMPLEX WITH ZINC,
AND MUTAGENESIS OF ASP-156.
PubMed=8961936; DOI=10.1021/bi962003n;
Romier C., Reuter K., Suck D., Ficner R.;
"Mutagenesis and crystallographic studies of Zymomonas mobilis tRNA-
guanine transglycosylase reveal aspartate 102 as the active site
nucleophile.";
Biochemistry 35:15734-15739(1996).
[6]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH ZINC.
PubMed=8654383;
Romier C., Reuter K., Suck D., Ficner R.;
"Crystal structure of tRNA-guanine transglycosylase: RNA modification
by base exchange.";
EMBO J. 15:2850-2857(1996).
[7]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 11-382 IN COMPLEX WITH ZINC,
AND MUTAGENESIS OF SER-103.
PubMed=10413112; DOI=10.1016/S0014-5793(99)00793-0;
Graedler U., Ficner R., Garcia G.A., Stubbs M.T., Klebe G., Reuter K.;
"Mutagenesis and crystallographic studies of Zymomonas mobilis tRNA-
guanine transglycosylase to elucidate the role of serine 103 for
enzymatic activity.";
FEBS Lett. 454:142-146(1999).
[8]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH ZINC.
PubMed=11178905; DOI=10.1006/jmbi.2000.4256;
Graedler U., Gerber H.-D., Goodenough-Lashua D.M., Garcia G.A.,
Ficner R., Reuter K., Stubbs M.T., Klebe G.;
"A new target for shigellosis: rational design and crystallographic
studies of inhibitors of tRNA-guanine transglycosylase.";
J. Mol. Biol. 306:455-467(2001).
[9]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 12-386 IN COMPLEX WITH ZINC.
PubMed=11921407;
DOI=10.1002/1439-7633(20020301)3:2/3<250::AID-CBIC250>3.0.CO;2-J;
Meyer E.A., Brenk R., Castellano R.K., Furler M., Klebe G.,
Diederich F.;
"De novo design, synthesis, and in vitro evaluation of inhibitors for
prokaryotic tRNA-guanine transglycosylase: a dramatic sulfur effect on
binding affinity.";
ChemBioChem 3:250-253(2002).
[10]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 2-383 OF MUTANT E-280 IN
COMPLEX WITH ZINC.
PubMed=12909636; DOI=10.1074/jbc.M304323200;
Kittendorf J.D., Sgraja T., Reuter K., Klebe G., Garcia G.A.;
"An essential role for aspartate 264 in catalysis by tRNA-guanine
transglycosylase from Escherichia coli.";
J. Biol. Chem. 278:42369-42376(2003).
[11]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH ZINC.
PubMed=14523925; DOI=10.1002/cbic.200300644;
Brenk R., Stubbs M.T., Heine A., Reuter K., Klebe G.;
"Flexible adaptations in the structure of the tRNA-modifying enzyme
tRNA-guanine transglycosylase and their implications for substrate
selectivity, reaction mechanism and structure-based drug design.";
ChemBioChem 4:1066-1077(2003).
[12]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 12-386 IN COMPLEX WITH ZINC.
PubMed=12646024; DOI=10.1021/jm0209937;
Brenk R., Naerum L., Graedler U., Gerber H.-D., Garcia G.A.,
Reuter K., Stubbs M.T., Klebe G.;
"Virtual screening for submicromolar leads of tRNA-guanine
transglycosylase based on a new unexpected binding mode detected by
crystal structure analysis.";
J. Med. Chem. 46:1133-1143(2003).
[13]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 1-386 IN COMPLEX WITH
9-DEAZAGUANINE AND ZINC, SUBUNIT, AND MUTAGENESIS OF ASP-280.
PubMed=12949492; DOI=10.1038/nsb976;
Xie W., Liu X., Huang R.H.;
"Chemical trapping and crystal structure of a catalytic tRNA guanine
transglycosylase covalent intermediate.";
Nat. Struct. Biol. 10:781-788(2003).
[14]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-386 IN COMPLEX WITH ZINC,
AND SUBUNIT.
PubMed=19627989; DOI=10.1016/j.jmb.2009.07.040;
Ritschel T., Atmanene C., Reuter K., Van Dorsselaer A.,
Sanglier-Cianferani S., Klebe G.;
"An integrative approach combining noncovalent mass spectrometry,
enzyme kinetics and X-ray crystallography to decipher Tgt protein-
protein and protein-RNA interaction.";
J. Mol. Biol. 393:833-847(2009).
-!- FUNCTION: 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).
{ECO:0000255|HAMAP-Rule:MF_00168, ECO:0000269|PubMed:7665516}.
-!- CATALYTIC ACTIVITY: Guanine(34) in tRNA + 7-aminomethyl-7-
carbaguanine = 7-aminomethyl-7-carbaguanine(34) in tRNA + guanine.
{ECO:0000255|HAMAP-Rule:MF_00168, ECO:0000269|PubMed:7665516}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000255|HAMAP-Rule:MF_00168,
ECO:0000269|PubMed:10413112, ECO:0000269|PubMed:11178905,
ECO:0000269|PubMed:11921407, ECO:0000269|PubMed:12646024,
ECO:0000269|PubMed:12909636, ECO:0000269|PubMed:12949492,
ECO:0000269|PubMed:14523925, ECO:0000269|PubMed:19627989,
ECO:0000269|PubMed:8654383, ECO:0000269|PubMed:8961936};
Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-
Rule:MF_00168, ECO:0000269|PubMed:10413112,
ECO:0000269|PubMed:11178905, ECO:0000269|PubMed:11921407,
ECO:0000269|PubMed:12646024, ECO:0000269|PubMed:12909636,
ECO:0000269|PubMed:12949492, ECO:0000269|PubMed:14523925,
ECO:0000269|PubMed:19627989, ECO:0000269|PubMed:8654383,
ECO:0000269|PubMed:8961936};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.2 uM for tRNA(Tyr) {ECO:0000269|PubMed:7665516};
KM=0.7 uM for guanine {ECO:0000269|PubMed:7665516};
Note=kcat is 0.0022 sec(-1) with tRNA(Tyr) and guanine as
substrates. {ECO:0000269|PubMed:7665516};
-!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
{ECO:0000255|HAMAP-Rule:MF_00168, ECO:0000305|PubMed:7665516}.
-!- SUBUNIT: Homodimer. Within each dimer, one monomer is responsible
for RNA recognition and catalysis, while the other monomer binds
to the replacement base PreQ1. {ECO:0000255|HAMAP-Rule:MF_00168,
ECO:0000269|PubMed:12949492, ECO:0000269|PubMed:19627989}.
-!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.
{ECO:0000255|HAMAP-Rule:MF_00168}.
-!- SEQUENCE CAUTION:
Sequence=AAA27704.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAA27705.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAG29862.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=Z11910; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
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EMBL; L33777; AAA27704.1; ALT_INIT; Genomic_DNA.
EMBL; L33777; AAA27705.1; ALT_INIT; Genomic_DNA.
EMBL; AF313764; AAG29862.1; ALT_INIT; Genomic_DNA.
EMBL; AE008692; AAV88987.2; -; Genomic_DNA.
EMBL; Z11910; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; T46898; T46898.
PDB; 1EFZ; X-ray; 2.00 A; A=1-386.
PDB; 1ENU; X-ray; 1.95 A; A=1-386.
PDB; 1F3E; X-ray; 1.85 A; A=1-386.
PDB; 1K4G; X-ray; 1.70 A; A=1-386.
PDB; 1K4H; X-ray; 1.80 A; A=1-386.
PDB; 1N2V; X-ray; 2.10 A; A=1-386.
PDB; 1OZM; X-ray; 1.95 A; A=2-386.
PDB; 1OZQ; X-ray; 1.90 A; A=2-386.
PDB; 1P0B; X-ray; 1.70 A; A=2-386.
PDB; 1P0D; X-ray; 1.90 A; A=2-386.
PDB; 1P0E; X-ray; 2.40 A; A=2-386.
PDB; 1PUD; X-ray; 1.85 A; A=1-386.
PDB; 1PXG; X-ray; 1.70 A; A=2-383.
PDB; 1Q2R; X-ray; 2.90 A; A/B/C/D=1-386.
PDB; 1Q2S; X-ray; 3.20 A; A/B/C/D=1-386.
PDB; 1Q4W; X-ray; 1.93 A; A=1-386.
PDB; 1Q63; X-ray; 1.85 A; A=1-386.
PDB; 1Q65; X-ray; 2.10 A; A=1-386.
PDB; 1Q66; X-ray; 1.75 A; A=1-386.
PDB; 1R5Y; X-ray; 1.20 A; A=1-386.
PDB; 1S38; X-ray; 1.81 A; A=1-386.
PDB; 1S39; X-ray; 1.95 A; A=1-386.
PDB; 1WKD; X-ray; 2.60 A; A=1-386.
PDB; 1WKE; X-ray; 2.20 A; A=1-386.
PDB; 1WKF; X-ray; 2.20 A; A=1-386.
PDB; 1Y5V; X-ray; 1.58 A; A=2-386.
PDB; 1Y5W; X-ray; 1.58 A; A=2-386.
PDB; 1Y5X; X-ray; 2.10 A; A/D=2-386.
PDB; 2BBF; X-ray; 1.70 A; A=1-386.
PDB; 2NQZ; X-ray; 1.46 A; A=2-386.
PDB; 2NSO; X-ray; 1.60 A; A=1-386.
PDB; 2OKO; X-ray; 1.50 A; A=2-386.
PDB; 2POT; X-ray; 1.80 A; A=1-386.
PDB; 2PWU; X-ray; 1.77 A; A=1-386.
PDB; 2PWV; X-ray; 1.70 A; A=1-386.
PDB; 2QII; X-ray; 1.70 A; A=1-386.
PDB; 2QZR; X-ray; 1.95 A; A=2-386.
PDB; 2Z1V; X-ray; 1.55 A; A=1-386.
PDB; 2Z1W; X-ray; 1.63 A; A=1-386.
PDB; 2Z1X; X-ray; 1.63 A; A=1-386.
PDB; 2Z7K; X-ray; 1.28 A; A=1-386.
PDB; 3BL3; X-ray; 2.25 A; A=1-386.
PDB; 3BLD; X-ray; 1.19 A; A=1-386.
PDB; 3BLL; X-ray; 1.26 A; A=1-386.
PDB; 3BLO; X-ray; 1.60 A; A=1-386.
PDB; 3C2Y; X-ray; 1.78 A; A=1-386.
PDB; 3EOS; X-ray; 1.78 A; A=1-386.
PDB; 3EOU; X-ray; 1.93 A; A=1-386.
PDB; 3GC4; X-ray; 1.80 A; A=1-386.
PDB; 3GC5; X-ray; 1.40 A; A=1-386.
PDB; 3GE7; X-ray; 1.50 A; A=1-386.
PDB; 3HFY; X-ray; 2.00 A; A=1-386.
PDB; 3RR4; X-ray; 1.68 A; A=1-386.
PDB; 3S1G; X-ray; 1.82 A; A=1-386.
PDB; 3SM0; X-ray; 1.57 A; A=1-386.
PDB; 3TLL; X-ray; 1.37 A; A=1-386.
PDB; 3UNT; X-ray; 1.80 A; A=1-386.
PDB; 3UVI; X-ray; 1.55 A; A=1-386.
PDB; 4DXX; X-ray; 1.66 A; A=1-386.
PDB; 4DY1; X-ray; 2.04 A; A=1-386.
PDB; 4E2V; X-ray; 1.18 A; A=1-386.
PDB; 4FPS; X-ray; 1.45 A; A=1-386.
PDB; 4FR1; X-ray; 1.74 A; A=1-386.
PDB; 4FR6; X-ray; 1.59 A; A=1-386.
PDB; 4FSA; X-ray; 1.62 A; A=1-386.
PDB; 4GCX; X-ray; 1.42 A; A=1-386.
PDB; 4GD0; X-ray; 1.29 A; A=1-386.
PDB; 4GG9; X-ray; 1.48 A; A=1-386.
PDB; 4GH1; X-ray; 1.45 A; A=1-386.
PDB; 4GH3; X-ray; 2.06 A; A=1-386.
PDB; 4GHR; X-ray; 2.00 A; A=1-386.
PDB; 4GI4; X-ray; 1.97 A; A=1-386.
PDB; 4GIY; X-ray; 1.75 A; A=1-386.
PDB; 4GKT; X-ray; 1.53 A; A=1-386.
PDB; 4H6E; X-ray; 1.42 A; A=1-386.
PDB; 4H7Z; X-ray; 1.68 A; A=1-386.
PDB; 4HQV; X-ray; 1.66 A; A=2-386.
PDB; 4HSH; X-ray; 1.56 A; A=2-386.
PDB; 4HTB; X-ray; 1.90 A; A=1-386.
PDB; 4HVX; X-ray; 1.82 A; A=1-386.
PDB; 4IPP; X-ray; 1.33 A; A=1-386.
PDB; 4JBR; X-ray; 2.92 A; A=1-386.
PDB; 4KWO; X-ray; 1.32 A; A=1-386.
PDB; 4L56; X-ray; 1.70 A; A=1-386.
PDB; 4LBU; X-ray; 1.17 A; A=1-386.
PDB; 4LEQ; X-ray; 1.40 A; A=1-386.
PDB; 4PUJ; X-ray; 1.42 A; A=1-386.
PDB; 4PUK; X-ray; 1.49 A; A=1-386.
PDB; 4PUL; X-ray; 1.65 A; A=1-386.
PDB; 4PUM; X-ray; 1.93 A; A=1-386.
PDB; 4PUN; X-ray; 1.25 A; A=1-386.
PDB; 4Q4M; X-ray; 1.62 A; A=1-386.
PDB; 4Q4O; X-ray; 1.35 A; A=1-386.
PDB; 4Q4P; X-ray; 1.54 A; A=1-386.
PDB; 4Q4Q; X-ray; 1.41 A; A=1-386.
PDB; 4Q4R; X-ray; 1.45 A; A=1-386.
PDB; 4Q4S; X-ray; 1.25 A; A=1-386.
PDB; 4Q8M; X-ray; 1.24 A; A=1-386.
PDB; 4Q8N; X-ray; 1.45 A; A=1-386.
PDB; 4Q8O; X-ray; 1.89 A; A=1-386.
PDB; 4Q8P; X-ray; 1.45 A; A=1-386.
PDB; 4Q8Q; X-ray; 1.72 A; A=1-386.
PDB; 4Q8T; X-ray; 1.40 A; A=1-386.
PDB; 4Q8U; X-ray; 1.31 A; A=1-386.
PDB; 4Q8V; X-ray; 1.40 A; A=1-386.
PDB; 4Q8W; X-ray; 1.14 A; A=1-386.
PDB; 5EGR; X-ray; 1.55 A; A=1-386.
PDB; 5I00; X-ray; 1.49 A; A=1-385.
PDB; 5I02; X-ray; 1.25 A; A=1-385.
PDB; 5I03; X-ray; 1.73 A; A=1-386.
PDB; 5I06; X-ray; 1.36 A; A=1-386.
PDB; 5I07; X-ray; 1.89 A; A/B=1-386.
PDB; 5I09; X-ray; 1.44 A; A=1-386.
PDB; 5J9M; X-ray; 1.33 A; A=1-386.
PDB; 5J9N; X-ray; 1.64 A; A=1-386.
PDB; 5J9O; X-ray; 1.41 A; A=1-386.
PDB; 5JGM; X-ray; 1.38 A; A=1-386.
PDB; 5JGO; X-ray; 1.37 A; A=1-386.
PDB; 5JSV; X-ray; 1.17 A; A=1-386.
PDB; 5JSW; X-ray; 1.22 A; A=1-386.
PDB; 5JT5; X-ray; 1.21 A; A=1-386.
PDB; 5JT6; X-ray; 1.54 A; A=1-386.
PDB; 5JT7; X-ray; 1.70 A; A=1-386.
PDB; 5JXQ; X-ray; 1.20 A; A=1-386.
PDB; 5LPO; X-ray; 1.42 A; A=1-386.
PDB; 5LPP; X-ray; 1.99 A; A=1-386.
PDB; 5LPQ; X-ray; 2.52 A; A/B=1-386.
PDB; 5LPS; X-ray; 1.27 A; A=1-386.
PDB; 5LPT; X-ray; 2.36 A; A/B=1-386.
PDB; 5SW3; X-ray; 1.38 A; A=10-384.
PDBsum; 1EFZ; -.
PDBsum; 1ENU; -.
PDBsum; 1F3E; -.
PDBsum; 1K4G; -.
PDBsum; 1K4H; -.
PDBsum; 1N2V; -.
PDBsum; 1OZM; -.
PDBsum; 1OZQ; -.
PDBsum; 1P0B; -.
PDBsum; 1P0D; -.
PDBsum; 1P0E; -.
PDBsum; 1PUD; -.
PDBsum; 1PXG; -.
PDBsum; 1Q2R; -.
PDBsum; 1Q2S; -.
PDBsum; 1Q4W; -.
PDBsum; 1Q63; -.
PDBsum; 1Q65; -.
PDBsum; 1Q66; -.
PDBsum; 1R5Y; -.
PDBsum; 1S38; -.
PDBsum; 1S39; -.
PDBsum; 1WKD; -.
PDBsum; 1WKE; -.
PDBsum; 1WKF; -.
PDBsum; 1Y5V; -.
PDBsum; 1Y5W; -.
PDBsum; 1Y5X; -.
PDBsum; 2BBF; -.
PDBsum; 2NQZ; -.
PDBsum; 2NSO; -.
PDBsum; 2OKO; -.
PDBsum; 2POT; -.
PDBsum; 2PWU; -.
PDBsum; 2PWV; -.
PDBsum; 2QII; -.
PDBsum; 2QZR; -.
PDBsum; 2Z1V; -.
PDBsum; 2Z1W; -.
PDBsum; 2Z1X; -.
PDBsum; 2Z7K; -.
PDBsum; 3BL3; -.
PDBsum; 3BLD; -.
PDBsum; 3BLL; -.
PDBsum; 3BLO; -.
PDBsum; 3C2Y; -.
PDBsum; 3EOS; -.
PDBsum; 3EOU; -.
PDBsum; 3GC4; -.
PDBsum; 3GC5; -.
PDBsum; 3GE7; -.
PDBsum; 3HFY; -.
PDBsum; 3RR4; -.
PDBsum; 3S1G; -.
PDBsum; 3SM0; -.
PDBsum; 3TLL; -.
PDBsum; 3UNT; -.
PDBsum; 3UVI; -.
PDBsum; 4DXX; -.
PDBsum; 4DY1; -.
PDBsum; 4E2V; -.
PDBsum; 4FPS; -.
PDBsum; 4FR1; -.
PDBsum; 4FR6; -.
PDBsum; 4FSA; -.
PDBsum; 4GCX; -.
PDBsum; 4GD0; -.
PDBsum; 4GG9; -.
PDBsum; 4GH1; -.
PDBsum; 4GH3; -.
PDBsum; 4GHR; -.
PDBsum; 4GI4; -.
PDBsum; 4GIY; -.
PDBsum; 4GKT; -.
PDBsum; 4H6E; -.
PDBsum; 4H7Z; -.
PDBsum; 4HQV; -.
PDBsum; 4HSH; -.
PDBsum; 4HTB; -.
PDBsum; 4HVX; -.
PDBsum; 4IPP; -.
PDBsum; 4JBR; -.
PDBsum; 4KWO; -.
PDBsum; 4L56; -.
PDBsum; 4LBU; -.
PDBsum; 4LEQ; -.
PDBsum; 4PUJ; -.
PDBsum; 4PUK; -.
PDBsum; 4PUL; -.
PDBsum; 4PUM; -.
PDBsum; 4PUN; -.
PDBsum; 4Q4M; -.
PDBsum; 4Q4O; -.
PDBsum; 4Q4P; -.
PDBsum; 4Q4Q; -.
PDBsum; 4Q4R; -.
PDBsum; 4Q4S; -.
PDBsum; 4Q8M; -.
PDBsum; 4Q8N; -.
PDBsum; 4Q8O; -.
PDBsum; 4Q8P; -.
PDBsum; 4Q8Q; -.
PDBsum; 4Q8T; -.
PDBsum; 4Q8U; -.
PDBsum; 4Q8V; -.
PDBsum; 4Q8W; -.
PDBsum; 5EGR; -.
PDBsum; 5I00; -.
PDBsum; 5I02; -.
PDBsum; 5I03; -.
PDBsum; 5I06; -.
PDBsum; 5I07; -.
PDBsum; 5I09; -.
PDBsum; 5J9M; -.
PDBsum; 5J9N; -.
PDBsum; 5J9O; -.
PDBsum; 5JGM; -.
PDBsum; 5JGO; -.
PDBsum; 5JSV; -.
PDBsum; 5JSW; -.
PDBsum; 5JT5; -.
PDBsum; 5JT6; -.
PDBsum; 5JT7; -.
PDBsum; 5JXQ; -.
PDBsum; 5LPO; -.
PDBsum; 5LPP; -.
PDBsum; 5LPQ; -.
PDBsum; 5LPS; -.
PDBsum; 5LPT; -.
PDBsum; 5SW3; -.
ProteinModelPortal; P28720; -.
SMR; P28720; -.
BindingDB; P28720; -.
ChEMBL; CHEMBL2987; -.
DrugBank; DB04239; 2-Amino-6-Aminomethyl-8-Phenylsulfanylmethyl-3h-Quinazolin-4-One.
DrugBank; DB01825; 2-Amino-8-Methylquinazolin-4(3h)-One.
DrugBank; DB03780; 2-Aminoquinazolin-4(3h)-One.
DrugBank; DB03304; 7-Deaza-7-Aminomethyl-Guanine.
DrugBank; DB03074; 7-Deaza-7-Cyano-Guanine.
DrugBank; DB02041; Isoluminol.
EnsemblBacteria; AAV88987; AAV88987; ZMO0363.
KEGG; zmo:ZMO0363; -.
HOGENOM; HOG000223473; -.
KO; K00773; -.
OMA; TYHLFLR; -.
BRENDA; 2.4.2.29; 6765.
UniPathway; UPA00392; -.
EvolutionaryTrace; P28720; -.
PRO; PR:P28720; -.
Proteomes; UP000001173; Chromosome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008479; F:queuine tRNA-ribosyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0101030; P:tRNA-guanine transglycosylation; IEA:InterPro.
Gene3D; 3.20.20.105; -; 1.
HAMAP; MF_00168; Q_tRNA_Tgt; 1.
InterPro; IPR004803; TGT.
InterPro; IPR036511; TGT-like_sf.
InterPro; IPR002616; tRNA_ribo_trans-like.
Pfam; PF01702; TGT; 1.
SUPFAM; SSF51713; SSF51713; 1.
TIGRFAMs; TIGR00430; Q_tRNA_tgt; 1.
TIGRFAMs; TIGR00449; tgt_general; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Glycosyltransferase; Metal-binding; Queuosine biosynthesis;
Reference proteome; Transferase; tRNA processing; Zinc.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:7665516}.
CHAIN 2 386 Queuine tRNA-ribosyltransferase.
/FTId=PRO_0000135563.
REGION 102 106 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_00168,
ECO:0000269|PubMed:12949492}.
REGION 261 267 RNA binding. {ECO:0000255|HAMAP-
Rule:MF_00168,
ECO:0000269|PubMed:12949492}.
REGION 285 289 RNA binding; important for wobble base 34
recognition. {ECO:0000255|HAMAP-
Rule:MF_00168,
ECO:0000269|PubMed:12949492}.
ACT_SITE 102 102 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_00168,
ECO:0000305|PubMed:12949492}.
ACT_SITE 280 280 Nucleophile. {ECO:0000255|HAMAP-
Rule:MF_00168,
ECO:0000305|PubMed:12949492}.
METAL 318 318 Zinc. {ECO:0000255|HAMAP-Rule:MF_00168,
ECO:0000269|PubMed:10413112,
ECO:0000269|PubMed:11178905,
ECO:0000269|PubMed:11921407,
ECO:0000269|PubMed:12646024,
ECO:0000269|PubMed:12909636,
ECO:0000269|PubMed:12949492,
ECO:0000269|PubMed:14523925,
ECO:0000269|PubMed:19627989,
ECO:0000269|PubMed:8654383,
ECO:0000269|PubMed:8961936}.
METAL 320 320 Zinc. {ECO:0000255|HAMAP-Rule:MF_00168,
ECO:0000269|PubMed:10413112,
ECO:0000269|PubMed:11178905,
ECO:0000269|PubMed:11921407,
ECO:0000269|PubMed:12646024,
ECO:0000269|PubMed:12909636,
ECO:0000269|PubMed:12949492,
ECO:0000269|PubMed:14523925,
ECO:0000269|PubMed:19627989,
ECO:0000269|PubMed:8654383,
ECO:0000269|PubMed:8961936}.
METAL 323 323 Zinc. {ECO:0000255|HAMAP-Rule:MF_00168,
ECO:0000269|PubMed:10413112,
ECO:0000269|PubMed:11178905,
ECO:0000269|PubMed:11921407,
ECO:0000269|PubMed:12646024,
ECO:0000269|PubMed:12909636,
ECO:0000269|PubMed:12949492,
ECO:0000269|PubMed:14523925,
ECO:0000269|PubMed:19627989,
ECO:0000269|PubMed:8654383,
ECO:0000269|PubMed:8961936}.
METAL 349 349 Zinc; via pros nitrogen.
{ECO:0000255|HAMAP-Rule:MF_00168,
ECO:0000269|PubMed:10413112,
ECO:0000269|PubMed:11178905,
ECO:0000269|PubMed:11921407,
ECO:0000269|PubMed:12646024,
ECO:0000269|PubMed:12909636,
ECO:0000269|PubMed:12949492,
ECO:0000269|PubMed:14523925,
ECO:0000269|PubMed:19627989,
ECO:0000269|PubMed:8654383,
ECO:0000269|PubMed:8961936}.
BINDING 156 156 Substrate. {ECO:0000255|HAMAP-
Rule:MF_00168,
ECO:0000269|PubMed:12949492}.
BINDING 203 203 Substrate. {ECO:0000255|HAMAP-
Rule:MF_00168,
ECO:0000269|PubMed:12949492}.
BINDING 230 230 Substrate; via amide nitrogen.
{ECO:0000255|HAMAP-Rule:MF_00168,
ECO:0000269|PubMed:12949492}.
MUTAGEN 103 103 S->A: Strongly reduces activity.
{ECO:0000269|PubMed:10413112}.
MUTAGEN 156 156 D->A: Abolishes catalytic activity.
{ECO:0000269|PubMed:8961936}.
MUTAGEN 280 280 D->N: Abolishes catalytic activity.
{ECO:0000269|PubMed:12949492}.
CONFLICT 312 312 T -> K (in Ref. 1 and 2). {ECO:0000305}.
STRAND 15 22 {ECO:0000244|PDB:4Q8W}.
STRAND 25 32 {ECO:0000244|PDB:4Q8W}.
STRAND 35 43 {ECO:0000244|PDB:4Q8W}.
STRAND 45 50 {ECO:0000244|PDB:3BLD}.
HELIX 56 61 {ECO:0000244|PDB:4Q8W}.
STRAND 63 65 {ECO:0000244|PDB:5I03}.
STRAND 67 70 {ECO:0000244|PDB:4Q8W}.
HELIX 71 76 {ECO:0000244|PDB:4Q8W}.
TURN 77 79 {ECO:0000244|PDB:2POT}.
HELIX 80 85 {ECO:0000244|PDB:4Q8W}.
HELIX 89 93 {ECO:0000244|PDB:4Q8W}.
STRAND 99 102 {ECO:0000244|PDB:4Q8W}.
HELIX 107 111 {ECO:0000244|PDB:4Q8W}.
HELIX 112 114 {ECO:0000244|PDB:4LBU}.
STRAND 115 117 {ECO:0000244|PDB:4LBU}.
STRAND 122 125 {ECO:0000244|PDB:4Q8W}.
TURN 127 129 {ECO:0000244|PDB:4Q8M}.
STRAND 132 135 {ECO:0000244|PDB:4Q8W}.
HELIX 137 147 {ECO:0000244|PDB:4Q8W}.
STRAND 150 153 {ECO:0000244|PDB:4Q8W}.
HELIX 165 188 {ECO:0000244|PDB:4Q8W}.
HELIX 190 195 {ECO:0000244|PDB:4Q8W}.
STRAND 197 202 {ECO:0000244|PDB:4Q8W}.
HELIX 208 221 {ECO:0000244|PDB:4Q8W}.
STRAND 224 228 {ECO:0000244|PDB:4Q8W}.
STRAND 232 234 {ECO:0000244|PDB:4Q8W}.
HELIX 237 247 {ECO:0000244|PDB:4Q8W}.
HELIX 248 250 {ECO:0000244|PDB:4Q8W}.
STRAND 253 255 {ECO:0000244|PDB:1P0E}.
STRAND 257 259 {ECO:0000244|PDB:4Q8W}.
HELIX 265 273 {ECO:0000244|PDB:4Q8W}.
STRAND 278 280 {ECO:0000244|PDB:4Q8W}.
HELIX 283 289 {ECO:0000244|PDB:4Q8W}.
STRAND 292 295 {ECO:0000244|PDB:5LPS}.
STRAND 298 301 {ECO:0000244|PDB:5LPS}.
HELIX 305 307 {ECO:0000244|PDB:4Q8W}.
STRAND 314 317 {ECO:0000244|PDB:4Q8W}.
HELIX 321 325 {ECO:0000244|PDB:4Q8W}.
HELIX 328 337 {ECO:0000244|PDB:4Q8W}.
HELIX 340 366 {ECO:0000244|PDB:4Q8W}.
HELIX 370 381 {ECO:0000244|PDB:4Q8W}.
SEQUENCE 386 AA; 42843 MW; 26754E08600BD941 CRC64;
MVEATAQETD RPRFSFSIAA REGKARTGTI EMKRGVIRTP AFMPVGTAAT VKALKPETVR
ATGADIILGN TYHLMLRPGA ERIAKLGGLH SFMGWDRPIL TDSGGYQVMS LSSLTKQSEE
GVTFKSHLDG SRHMLSPERS IEIQHLLGSD IVMAFDECTP YPATPSRAAS SMERSMRWAK
RSRDAFDSRK EQAENAALFG IQQGSVFENL RQQSADALAE IGFDGYAVGG LAVGEGQDEM
FRVLDFSVPM LPDDKPHYLM GVGKPDDIVG AVERGIDMFD CVLPTRSGRN GQAFTWDGPI
NIRNARFSED LTPLDSECHC AVCQKWSRAY IHHLIRAGEI LGAMLMTEHN IAFYQQLMQK
IRDSISEGRF SQFAQDFRAR YFARNS


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