TGT_ZYMMO
ID TGT_ZYMMO Reviewed; 386 AA.
AC P28720; Q5NQL7; Q60247; Q9F5L7;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Queuine tRNA-ribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00168};
DE EC=2.4.2.29 {ECO:0000255|HAMAP-Rule:MF_00168};
DE AltName: Full=Guanine insertion enzyme {ECO:0000255|HAMAP-Rule:MF_00168};
DE AltName: Full=tRNA-guanine transglycosylase {ECO:0000255|HAMAP-Rule:MF_00168};
GN Name=tgt {ECO:0000255|HAMAP-Rule:MF_00168}; OrderedLocusNames=ZMO0363;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-7, FUNCTION,
RP CATALYTIC ACTIVITY, PATHWAY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=7665516; DOI=10.1128/jb.177.18.5284-5288.1995;
RA Reuter K.K.H., Ficner R.;
RT "Sequence analysis and overexpression of the Zymomonas mobilis tgt gene
RT encoding tRNA-guanine transglycosylase: purification and biochemical
RT characterization of the enzyme.";
RL J. Bacteriol. 177:5284-5288(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RA Ahn J.Y., Kang H.S.;
RT "Sequence analysis of 44B6 fosmid clone of Zymomonas mobilis ZM4.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
RN [4]
RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=1526462; DOI=10.1016/0378-1097(92)90450-3;
RA Shark K.B., Conway T.;
RT "Cloning and molecular characterization of the DNA ligase gene (lig) from
RT Zymomonas mobilis.";
RL FEMS Microbiol. Lett. 75:19-26(1992).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-386 IN COMPLEX WITH ZINC, AND
RP MUTAGENESIS OF ASP-156.
RX PubMed=8961936; DOI=10.1021/bi962003n;
RA Romier C., Reuter K., Suck D., Ficner R.;
RT "Mutagenesis and crystallographic studies of Zymomonas mobilis tRNA-guanine
RT transglycosylase reveal aspartate 102 as the active site nucleophile.";
RL Biochemistry 35:15734-15739(1996).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH ZINC.
RX PubMed=8654383; DOI=10.1002/j.1460-2075.1996.tb00646.x;
RA Romier C., Reuter K., Suck D., Ficner R.;
RT "Crystal structure of tRNA-guanine transglycosylase: RNA modification by
RT base exchange.";
RL EMBO J. 15:2850-2857(1996).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 11-382 IN COMPLEX WITH ZINC, AND
RP MUTAGENESIS OF SER-103.
RX PubMed=10413112; DOI=10.1016/s0014-5793(99)00793-0;
RA Graedler U., Ficner R., Garcia G.A., Stubbs M.T., Klebe G., Reuter K.;
RT "Mutagenesis and crystallographic studies of Zymomonas mobilis tRNA-guanine
RT transglycosylase to elucidate the role of serine 103 for enzymatic
RT activity.";
RL FEBS Lett. 454:142-146(1999).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH ZINC.
RX PubMed=11178905; DOI=10.1006/jmbi.2000.4256;
RA Graedler U., Gerber H.-D., Goodenough-Lashua D.M., Garcia G.A., Ficner R.,
RA Reuter K., Stubbs M.T., Klebe G.;
RT "A new target for shigellosis: rational design and crystallographic studies
RT of inhibitors of tRNA-guanine transglycosylase.";
RL J. Mol. Biol. 306:455-467(2001).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 12-386 IN COMPLEX WITH ZINC.
RX PubMed=11921407;
RX DOI=10.1002/1439-7633(20020301)3:2/3<250::aid-cbic250>3.0.co;2-j;
RA Meyer E.A., Brenk R., Castellano R.K., Furler M., Klebe G., Diederich F.;
RT "De novo design, synthesis, and in vitro evaluation of inhibitors for
RT prokaryotic tRNA-guanine transglycosylase: a dramatic sulfur effect on
RT binding affinity.";
RL ChemBioChem 3:250-253(2002).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 2-383 OF MUTANT E-280 IN COMPLEX
RP WITH ZINC.
RX PubMed=12909636; DOI=10.1074/jbc.m304323200;
RA Kittendorf J.D., Sgraja T., Reuter K., Klebe G., Garcia G.A.;
RT "An essential role for aspartate 264 in catalysis by tRNA-guanine
RT transglycosylase from Escherichia coli.";
RL J. Biol. Chem. 278:42369-42376(2003).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH ZINC.
RX PubMed=14523925; DOI=10.1002/cbic.200300644;
RA Brenk R., Stubbs M.T., Heine A., Reuter K., Klebe G.;
RT "Flexible adaptations in the structure of the tRNA-modifying enzyme tRNA-
RT guanine transglycosylase and their implications for substrate selectivity,
RT reaction mechanism and structure-based drug design.";
RL ChemBioChem 4:1066-1077(2003).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 12-386 IN COMPLEX WITH ZINC.
RX PubMed=12646024; DOI=10.1021/jm0209937;
RA Brenk R., Naerum L., Graedler U., Gerber H.-D., Garcia G.A., Reuter K.,
RA Stubbs M.T., Klebe G.;
RT "Virtual screening for submicromolar leads of tRNA-guanine transglycosylase
RT based on a new unexpected binding mode detected by crystal structure
RT analysis.";
RL J. Med. Chem. 46:1133-1143(2003).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 1-386 IN COMPLEX WITH
RP 9-DEAZAGUANINE AND ZINC, SUBUNIT, AND MUTAGENESIS OF ASP-280.
RX PubMed=12949492; DOI=10.1038/nsb976;
RA Xie W., Liu X., Huang R.H.;
RT "Chemical trapping and crystal structure of a catalytic tRNA guanine
RT transglycosylase covalent intermediate.";
RL Nat. Struct. Biol. 10:781-788(2003).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-386 IN COMPLEX WITH ZINC, AND
RP SUBUNIT.
RX PubMed=19627989; DOI=10.1016/j.jmb.2009.07.040;
RA Ritschel T., Atmanene C., Reuter K., Van Dorsselaer A.,
RA Sanglier-Cianferani S., Klebe G.;
RT "An integrative approach combining noncovalent mass spectrometry, enzyme
RT kinetics and X-ray crystallography to decipher Tgt protein-protein and
RT protein-RNA interaction.";
RL J. Mol. Biol. 393:833-847(2009).
CC -!- FUNCTION: Catalyzes the base-exchange of a guanine (G) residue with the
CC queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34
CC (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp,
CC -Asn, -His and -Tyr). Catalysis occurs through a double-displacement
CC mechanism. The nucleophile active site attacks the C1' of nucleotide 34
CC to detach the guanine base from the RNA, forming a covalent enzyme-RNA
CC intermediate. The proton acceptor active site deprotonates the incoming
CC PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form
CC the product. After dissociation, two additional enzymatic reactions on
CC the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified
CC nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-
CC yl)amino)methyl)-7-deazaguanosine). {ECO:0000255|HAMAP-Rule:MF_00168,
CC ECO:0000269|PubMed:7665516}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-aminomethyl-7-carbaguanine + guanosine(34) in tRNA = 7-
CC aminomethyl-7-carbaguanosine(34) in tRNA + guanine;
CC Xref=Rhea:RHEA:24104, Rhea:RHEA-COMP:10341, Rhea:RHEA-COMP:10342,
CC ChEBI:CHEBI:16235, ChEBI:CHEBI:58703, ChEBI:CHEBI:74269,
CC ChEBI:CHEBI:82833; EC=2.4.2.29; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00168, ECO:0000269|PubMed:7665516};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00168,
CC ECO:0000269|PubMed:10413112, ECO:0000269|PubMed:11178905,
CC ECO:0000269|PubMed:11921407, ECO:0000269|PubMed:12646024,
CC ECO:0000269|PubMed:12909636, ECO:0000269|PubMed:12949492,
CC ECO:0000269|PubMed:14523925, ECO:0000269|PubMed:19627989,
CC ECO:0000269|PubMed:8654383, ECO:0000269|PubMed:8961936};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00168,
CC ECO:0000269|PubMed:10413112, ECO:0000269|PubMed:11178905,
CC ECO:0000269|PubMed:11921407, ECO:0000269|PubMed:12646024,
CC ECO:0000269|PubMed:12909636, ECO:0000269|PubMed:12949492,
CC ECO:0000269|PubMed:14523925, ECO:0000269|PubMed:19627989,
CC ECO:0000269|PubMed:8654383, ECO:0000269|PubMed:8961936};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.2 uM for tRNA(Tyr) {ECO:0000269|PubMed:7665516};
CC KM=0.7 uM for guanine {ECO:0000269|PubMed:7665516};
CC Note=kcat is 0.0022 sec(-1) with tRNA(Tyr) and guanine as substrates.
CC {ECO:0000269|PubMed:7665516};
CC -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00168, ECO:0000305|PubMed:7665516}.
CC -!- SUBUNIT: Homodimer. Within each dimer, one monomer is responsible for
CC RNA recognition and catalysis, while the other monomer binds to the
CC replacement base PreQ1. {ECO:0000255|HAMAP-Rule:MF_00168,
CC ECO:0000269|PubMed:12949492, ECO:0000269|PubMed:19627989}.
CC -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_00168}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA27704.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAA27705.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAG29862.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=Z11910; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L33777; AAA27704.1; ALT_INIT; Genomic_DNA.
DR EMBL; L33777; AAA27705.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF313764; AAG29862.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE008692; AAV88987.2; -; Genomic_DNA.
DR EMBL; Z11910; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; T46898; T46898.
DR PDB; 1EFZ; X-ray; 2.00 A; A=1-386.
DR PDB; 1ENU; X-ray; 1.95 A; A=1-386.
DR PDB; 1F3E; X-ray; 1.85 A; A=1-386.
DR PDB; 1K4G; X-ray; 1.70 A; A=1-386.
DR PDB; 1K4H; X-ray; 1.80 A; A=1-386.
DR PDB; 1N2V; X-ray; 2.10 A; A=1-386.
DR PDB; 1OZM; X-ray; 1.95 A; A=2-386.
DR PDB; 1OZQ; X-ray; 1.90 A; A=2-386.
DR PDB; 1P0B; X-ray; 1.70 A; A=2-386.
DR PDB; 1P0D; X-ray; 1.90 A; A=2-386.
DR PDB; 1P0E; X-ray; 2.40 A; A=2-386.
DR PDB; 1PUD; X-ray; 1.85 A; A=1-386.
DR PDB; 1PXG; X-ray; 1.70 A; A=2-383.
DR PDB; 1Q2R; X-ray; 2.90 A; A/B/C/D=1-386.
DR PDB; 1Q2S; X-ray; 3.20 A; A/B/C/D=1-386.
DR PDB; 1Q4W; X-ray; 1.93 A; A=1-386.
DR PDB; 1Q63; X-ray; 1.85 A; A=1-386.
DR PDB; 1Q65; X-ray; 2.10 A; A=1-386.
DR PDB; 1Q66; X-ray; 1.75 A; A=1-386.
DR PDB; 1R5Y; X-ray; 1.20 A; A=1-386.
DR PDB; 1S38; X-ray; 1.81 A; A=1-386.
DR PDB; 1S39; X-ray; 1.95 A; A=1-386.
DR PDB; 1WKD; X-ray; 2.60 A; A=1-386.
DR PDB; 1WKE; X-ray; 2.20 A; A=1-386.
DR PDB; 1WKF; X-ray; 2.20 A; A=1-386.
DR PDB; 1Y5V; X-ray; 1.58 A; A=2-386.
DR PDB; 1Y5W; X-ray; 1.58 A; A=2-386.
DR PDB; 1Y5X; X-ray; 2.10 A; A/D=2-386.
DR PDB; 2BBF; X-ray; 1.70 A; A=1-386.
DR PDB; 2NQZ; X-ray; 1.46 A; A=2-386.
DR PDB; 2NSO; X-ray; 1.60 A; A=1-386.
DR PDB; 2OKO; X-ray; 1.50 A; A=2-386.
DR PDB; 2POT; X-ray; 1.80 A; A=1-386.
DR PDB; 2PWU; X-ray; 1.77 A; A=1-386.
DR PDB; 2PWV; X-ray; 1.70 A; A=1-386.
DR PDB; 2QII; X-ray; 1.70 A; A=1-386.
DR PDB; 2QZR; X-ray; 1.95 A; A=2-386.
DR PDB; 2Z1V; X-ray; 1.55 A; A=1-386.
DR PDB; 2Z1W; X-ray; 1.63 A; A=1-386.
DR PDB; 2Z1X; X-ray; 1.63 A; A=1-386.
DR PDB; 2Z7K; X-ray; 1.28 A; A=1-386.
DR PDB; 3BL3; X-ray; 2.25 A; A=1-386.
DR PDB; 3BLD; X-ray; 1.19 A; A=1-386.
DR PDB; 3BLL; X-ray; 1.26 A; A=1-386.
DR PDB; 3BLO; X-ray; 1.60 A; A=1-386.
DR PDB; 3C2Y; X-ray; 1.78 A; A=1-386.
DR PDB; 3EOS; X-ray; 1.78 A; A=1-386.
DR PDB; 3EOU; X-ray; 1.93 A; A=1-386.
DR PDB; 3GC4; X-ray; 1.80 A; A=1-386.
DR PDB; 3GC5; X-ray; 1.40 A; A=1-386.
DR PDB; 3GE7; X-ray; 1.50 A; A=1-386.
DR PDB; 3HFY; X-ray; 2.00 A; A=1-386.
DR PDB; 3RR4; X-ray; 1.68 A; A=1-386.
DR PDB; 3S1G; X-ray; 1.82 A; A=1-386.
DR PDB; 3SM0; X-ray; 1.57 A; A=1-386.
DR PDB; 3TLL; X-ray; 1.37 A; A=1-386.
DR PDB; 3UNT; X-ray; 1.80 A; A=1-386.
DR PDB; 3UVI; X-ray; 1.55 A; A=1-386.
DR PDB; 4DXX; X-ray; 1.66 A; A=1-386.
DR PDB; 4DY1; X-ray; 2.04 A; A=1-386.
DR PDB; 4E2V; X-ray; 1.18 A; A=1-386.
DR PDB; 4FPS; X-ray; 1.45 A; A=1-386.
DR PDB; 4FR1; X-ray; 1.74 A; A=1-386.
DR PDB; 4FR6; X-ray; 1.59 A; A=1-386.
DR PDB; 4FSA; X-ray; 1.62 A; A=1-386.
DR PDB; 4GCX; X-ray; 1.42 A; A=1-386.
DR PDB; 4GD0; X-ray; 1.29 A; A=1-386.
DR PDB; 4GG9; X-ray; 1.48 A; A=1-386.
DR PDB; 4GH1; X-ray; 1.45 A; A=1-386.
DR PDB; 4GH3; X-ray; 2.06 A; A=1-386.
DR PDB; 4GHR; X-ray; 2.00 A; A=1-386.
DR PDB; 4GI4; X-ray; 1.97 A; A=1-386.
DR PDB; 4GIY; X-ray; 1.75 A; A=1-386.
DR PDB; 4GKT; X-ray; 1.53 A; A=1-386.
DR PDB; 4H6E; X-ray; 1.42 A; A=1-386.
DR PDB; 4H7Z; X-ray; 1.68 A; A=1-386.
DR PDB; 4HQV; X-ray; 1.66 A; A=2-386.
DR PDB; 4HSH; X-ray; 1.56 A; A=2-386.
DR PDB; 4HTB; X-ray; 1.90 A; A=1-386.
DR PDB; 4HVX; X-ray; 1.82 A; A=1-386.
DR PDB; 4IPP; X-ray; 1.33 A; A=1-386.
DR PDB; 4JBR; X-ray; 2.92 A; A=1-386.
DR PDB; 4KWO; X-ray; 1.32 A; A=1-386.
DR PDB; 4L56; X-ray; 1.70 A; A=1-386.
DR PDB; 4LBU; X-ray; 1.17 A; A=1-386.
DR PDB; 4LEQ; X-ray; 1.40 A; A=1-386.
DR PDB; 4PUJ; X-ray; 1.42 A; A=1-386.
DR PDB; 4PUK; X-ray; 1.49 A; A=1-386.
DR PDB; 4PUL; X-ray; 1.65 A; A=1-386.
DR PDB; 4PUM; X-ray; 1.93 A; A=1-386.
DR PDB; 4PUN; X-ray; 1.25 A; A=1-386.
DR PDB; 4Q4M; X-ray; 1.62 A; A=1-386.
DR PDB; 4Q4O; X-ray; 1.35 A; A=1-386.
DR PDB; 4Q4P; X-ray; 1.54 A; A=1-386.
DR PDB; 4Q4Q; X-ray; 1.41 A; A=1-386.
DR PDB; 4Q4R; X-ray; 1.45 A; A=1-386.
DR PDB; 4Q4S; X-ray; 1.25 A; A=1-386.
DR PDB; 4Q8M; X-ray; 1.24 A; A=1-386.
DR PDB; 4Q8N; X-ray; 1.45 A; A=1-386.
DR PDB; 4Q8O; X-ray; 1.89 A; A=1-386.
DR PDB; 4Q8P; X-ray; 1.45 A; A=1-386.
DR PDB; 4Q8Q; X-ray; 1.72 A; A=1-386.
DR PDB; 4Q8T; X-ray; 1.40 A; A=1-386.
DR PDB; 4Q8U; X-ray; 1.31 A; A=1-386.
DR PDB; 4Q8V; X-ray; 1.40 A; A=1-386.
DR PDB; 4Q8W; X-ray; 1.14 A; A=1-386.
DR PDB; 5EGR; X-ray; 1.55 A; A=1-386.
DR PDB; 5I00; X-ray; 1.49 A; A=1-385.
DR PDB; 5I02; X-ray; 1.25 A; A=1-385.
DR PDB; 5I03; X-ray; 1.73 A; A=1-386.
DR PDB; 5I06; X-ray; 1.36 A; A=1-386.
DR PDB; 5I07; X-ray; 1.89 A; A/B=1-386.
DR PDB; 5I09; X-ray; 1.44 A; A=1-386.
DR PDB; 5J9M; X-ray; 1.33 A; A=1-386.
DR PDB; 5J9N; X-ray; 1.64 A; A=1-386.
DR PDB; 5J9O; X-ray; 1.41 A; A=1-386.
DR PDB; 5JGM; X-ray; 1.38 A; A=1-386.
DR PDB; 5JGO; X-ray; 1.37 A; A=1-386.
DR PDB; 5JSV; X-ray; 1.17 A; A=1-386.
DR PDB; 5JSW; X-ray; 1.22 A; A=1-386.
DR PDB; 5JT5; X-ray; 1.21 A; A=1-386.
DR PDB; 5JT6; X-ray; 1.54 A; A=1-386.
DR PDB; 5JT7; X-ray; 1.70 A; A=1-386.
DR PDB; 5JXQ; X-ray; 1.20 A; A=1-386.
DR PDB; 5LPO; X-ray; 1.42 A; A=1-386.
DR PDB; 5LPP; X-ray; 1.99 A; A=1-386.
DR PDB; 5LPQ; X-ray; 2.52 A; A/B=1-386.
DR PDB; 5LPS; X-ray; 1.27 A; A=1-386.
DR PDB; 5LPT; X-ray; 2.36 A; A/B=1-386.
DR PDB; 5N6F; X-ray; 1.12 A; A=10-384.
DR PDB; 5SW3; X-ray; 1.38 A; A=10-384.
DR PDB; 5UTI; X-ray; 1.36 A; A=10-384.
DR PDB; 5UTJ; X-ray; 1.55 A; A=10-384.
DR PDB; 5V3C; X-ray; 1.42 A; A=10-384.
DR PDB; 6FMN; X-ray; 1.36 A; A=1-386.
DR PDB; 6FPU; X-ray; 1.36 A; A=1-386.
DR PDB; 6FSO; X-ray; 1.45 A; A=10-384.
DR PDB; 6H7C; X-ray; 1.68 A; A=1-386.
DR PDB; 6RKQ; X-ray; 1.67 A; A=10-384.
DR PDB; 6RKT; X-ray; 1.75 A; A=10-384.
DR PDB; 6YFW; X-ray; 1.26 A; A=1-386.
DR PDB; 6YFX; X-ray; 1.38 A; A=1-386.
DR PDB; 6YGK; X-ray; 1.40 A; A=1-386.
DR PDB; 6YGL; X-ray; 1.48 A; A=1-386.
DR PDB; 6YGM; X-ray; 1.23 A; A=1-386.
DR PDB; 6YGO; X-ray; 1.26 A; A=1-386.
DR PDB; 6YGP; X-ray; 1.33 A; A=1-386.
DR PDB; 6YGR; X-ray; 1.70 A; A=1-386.
DR PDB; 6YGS; X-ray; 1.40 A; A=1-386.
DR PDB; 6YGV; X-ray; 1.63 A; A=1-386.
DR PDB; 6YGW; X-ray; 1.16 A; A=1-386.
DR PDB; 6YGX; X-ray; 1.35 A; A=1-386.
DR PDB; 6YGY; X-ray; 1.52 A; A=1-386.
DR PDB; 6YGZ; X-ray; 1.86 A; A=1-386.
DR PDB; 6YH1; X-ray; 1.55 A; A=1-386.
DR PDB; 6YH2; X-ray; 1.19 A; A=1-386.
DR PDB; 6YH3; X-ray; 1.49 A; A=1-386.
DR PDB; 6YHD; X-ray; 1.25 A; A=1-386.
DR PDB; 6YHE; X-ray; 1.54 A; A=1-386.
DR PDB; 6YIQ; X-ray; 1.58 A; A/B=1-386.
DR PDB; 6YRY; X-ray; 1.82 A; A=1-386.
DR PDB; 6YYZ; X-ray; 1.21 A; A=1-386.
DR PDB; 6Z0D; X-ray; 1.65 A; A=1-386.
DR PDB; 7A0B; X-ray; 1.77 A; A=1-386.
DR PDB; 7A3V; X-ray; 1.70 A; A=1-386.
DR PDB; 7A3X; X-ray; 1.85 A; A=1-386.
DR PDB; 7A4K; X-ray; 1.68 A; A=1-386.
DR PDB; 7A4X; X-ray; 2.05 A; A=1-386.
DR PDB; 7A6D; X-ray; 1.59 A; A=1-386.
DR PDB; 7A9E; X-ray; 1.76 A; A=1-386.
DR PDB; 7ADN; X-ray; 1.92 A; A=1-386.
DR PDB; 7APL; X-ray; 1.99 A; A=1-386.
DR PDB; 7APM; X-ray; 1.66 A; A=1-386.
DR PDBsum; 1EFZ; -.
DR PDBsum; 1ENU; -.
DR PDBsum; 1F3E; -.
DR PDBsum; 1K4G; -.
DR PDBsum; 1K4H; -.
DR PDBsum; 1N2V; -.
DR PDBsum; 1OZM; -.
DR PDBsum; 1OZQ; -.
DR PDBsum; 1P0B; -.
DR PDBsum; 1P0D; -.
DR PDBsum; 1P0E; -.
DR PDBsum; 1PUD; -.
DR PDBsum; 1PXG; -.
DR PDBsum; 1Q2R; -.
DR PDBsum; 1Q2S; -.
DR PDBsum; 1Q4W; -.
DR PDBsum; 1Q63; -.
DR PDBsum; 1Q65; -.
DR PDBsum; 1Q66; -.
DR PDBsum; 1R5Y; -.
DR PDBsum; 1S38; -.
DR PDBsum; 1S39; -.
DR PDBsum; 1WKD; -.
DR PDBsum; 1WKE; -.
DR PDBsum; 1WKF; -.
DR PDBsum; 1Y5V; -.
DR PDBsum; 1Y5W; -.
DR PDBsum; 1Y5X; -.
DR PDBsum; 2BBF; -.
DR PDBsum; 2NQZ; -.
DR PDBsum; 2NSO; -.
DR PDBsum; 2OKO; -.
DR PDBsum; 2POT; -.
DR PDBsum; 2PWU; -.
DR PDBsum; 2PWV; -.
DR PDBsum; 2QII; -.
DR PDBsum; 2QZR; -.
DR PDBsum; 2Z1V; -.
DR PDBsum; 2Z1W; -.
DR PDBsum; 2Z1X; -.
DR PDBsum; 2Z7K; -.
DR PDBsum; 3BL3; -.
DR PDBsum; 3BLD; -.
DR PDBsum; 3BLL; -.
DR PDBsum; 3BLO; -.
DR PDBsum; 3C2Y; -.
DR PDBsum; 3EOS; -.
DR PDBsum; 3EOU; -.
DR PDBsum; 3GC4; -.
DR PDBsum; 3GC5; -.
DR PDBsum; 3GE7; -.
DR PDBsum; 3HFY; -.
DR PDBsum; 3RR4; -.
DR PDBsum; 3S1G; -.
DR PDBsum; 3SM0; -.
DR PDBsum; 3TLL; -.
DR PDBsum; 3UNT; -.
DR PDBsum; 3UVI; -.
DR PDBsum; 4DXX; -.
DR PDBsum; 4DY1; -.
DR PDBsum; 4E2V; -.
DR PDBsum; 4FPS; -.
DR PDBsum; 4FR1; -.
DR PDBsum; 4FR6; -.
DR PDBsum; 4FSA; -.
DR PDBsum; 4GCX; -.
DR PDBsum; 4GD0; -.
DR PDBsum; 4GG9; -.
DR PDBsum; 4GH1; -.
DR PDBsum; 4GH3; -.
DR PDBsum; 4GHR; -.
DR PDBsum; 4GI4; -.
DR PDBsum; 4GIY; -.
DR PDBsum; 4GKT; -.
DR PDBsum; 4H6E; -.
DR PDBsum; 4H7Z; -.
DR PDBsum; 4HQV; -.
DR PDBsum; 4HSH; -.
DR PDBsum; 4HTB; -.
DR PDBsum; 4HVX; -.
DR PDBsum; 4IPP; -.
DR PDBsum; 4JBR; -.
DR PDBsum; 4KWO; -.
DR PDBsum; 4L56; -.
DR PDBsum; 4LBU; -.
DR PDBsum; 4LEQ; -.
DR PDBsum; 4PUJ; -.
DR PDBsum; 4PUK; -.
DR PDBsum; 4PUL; -.
DR PDBsum; 4PUM; -.
DR PDBsum; 4PUN; -.
DR PDBsum; 4Q4M; -.
DR PDBsum; 4Q4O; -.
DR PDBsum; 4Q4P; -.
DR PDBsum; 4Q4Q; -.
DR PDBsum; 4Q4R; -.
DR PDBsum; 4Q4S; -.
DR PDBsum; 4Q8M; -.
DR PDBsum; 4Q8N; -.
DR PDBsum; 4Q8O; -.
DR PDBsum; 4Q8P; -.
DR PDBsum; 4Q8Q; -.
DR PDBsum; 4Q8T; -.
DR PDBsum; 4Q8U; -.
DR PDBsum; 4Q8V; -.
DR PDBsum; 4Q8W; -.
DR PDBsum; 5EGR; -.
DR PDBsum; 5I00; -.
DR PDBsum; 5I02; -.
DR PDBsum; 5I03; -.
DR PDBsum; 5I06; -.
DR PDBsum; 5I07; -.
DR PDBsum; 5I09; -.
DR PDBsum; 5J9M; -.
DR PDBsum; 5J9N; -.
DR PDBsum; 5J9O; -.
DR PDBsum; 5JGM; -.
DR PDBsum; 5JGO; -.
DR PDBsum; 5JSV; -.
DR PDBsum; 5JSW; -.
DR PDBsum; 5JT5; -.
DR PDBsum; 5JT6; -.
DR PDBsum; 5JT7; -.
DR PDBsum; 5JXQ; -.
DR PDBsum; 5LPO; -.
DR PDBsum; 5LPP; -.
DR PDBsum; 5LPQ; -.
DR PDBsum; 5LPS; -.
DR PDBsum; 5LPT; -.
DR PDBsum; 5N6F; -.
DR PDBsum; 5SW3; -.
DR PDBsum; 5UTI; -.
DR PDBsum; 5UTJ; -.
DR PDBsum; 5V3C; -.
DR PDBsum; 6FMN; -.
DR PDBsum; 6FPU; -.
DR PDBsum; 6FSO; -.
DR PDBsum; 6H7C; -.
DR PDBsum; 6RKQ; -.
DR PDBsum; 6RKT; -.
DR PDBsum; 6YFW; -.
DR PDBsum; 6YFX; -.
DR PDBsum; 6YGK; -.
DR PDBsum; 6YGL; -.
DR PDBsum; 6YGM; -.
DR PDBsum; 6YGO; -.
DR PDBsum; 6YGP; -.
DR PDBsum; 6YGR; -.
DR PDBsum; 6YGS; -.
DR PDBsum; 6YGV; -.
DR PDBsum; 6YGW; -.
DR PDBsum; 6YGX; -.
DR PDBsum; 6YGY; -.
DR PDBsum; 6YGZ; -.
DR PDBsum; 6YH1; -.
DR PDBsum; 6YH2; -.
DR PDBsum; 6YH3; -.
DR PDBsum; 6YHD; -.
DR PDBsum; 6YHE; -.
DR PDBsum; 6YIQ; -.
DR PDBsum; 6YRY; -.
DR PDBsum; 6YYZ; -.
DR PDBsum; 6Z0D; -.
DR PDBsum; 7A0B; -.
DR PDBsum; 7A3V; -.
DR PDBsum; 7A3X; -.
DR PDBsum; 7A4K; -.
DR PDBsum; 7A4X; -.
DR PDBsum; 7A6D; -.
DR PDBsum; 7A9E; -.
DR PDBsum; 7ADN; -.
DR PDBsum; 7APL; -.
DR PDBsum; 7APM; -.
DR AlphaFoldDB; P28720; -.
DR SMR; P28720; -.
DR STRING; 264203.ZMO0363; -.
DR BindingDB; P28720; -.
DR ChEMBL; CHEMBL2987; -.
DR DrugBank; DB07452; 2,6-diamino-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one.
DR DrugBank; DB04543; 2,6-Diamino-8-(1h-Imidazol-2-Ylsulfanylmethyl)-3h-Quinazoline-4-One.
DR DrugBank; DB04004; 2,6-Diamino-8-(2-Dimethylaminoethylsulfanylmethyl)-3h-Quinazolin-4-One.
DR DrugBank; DB02599; 2,6-Diamino-8-Propylsulfanylmethyl-3h-Quinazoline-4-One.
DR DrugBank; DB03505; 2,6-diaminoquinazolin-4-ol.
DR DrugBank; DB04239; 2-Amino-6-Aminomethyl-8-Phenylsulfanylmethyl-3h-Quinazolin-4-One.
DR DrugBank; DB01825; 2-amino-8-methyl-4(1H)-quinazolinone.
DR DrugBank; DB03780; 2-Aminoquinazolin-4(3h)-One.
DR DrugBank; DB02441; 2-Butyl-5,6-Dihydro-1h-Imidazo[4,5-D]Pyridazine-4,7-Dione.
DR DrugBank; DB04169; 3,5-Diaminophthalhydrazide.
DR DrugBank; DB08512; 6-amino-2-[(1-naphthylmethyl)amino]-3,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one.
DR DrugBank; DB07564; 6-amino-2-[(2-morpholin-4-ylethyl)amino]-3,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one.
DR DrugBank; DB08514; 6-amino-2-[(thiophen-2-ylmethyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one.
DR DrugBank; DB08511; 6-amino-2-methyl-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one.
DR DrugBank; DB07012; 6-AMINO-3,7-DIHYDRO-IMIDAZO[4,5-G]QUINAZOLIN-8-ONE.
DR DrugBank; DB08267; 6-amino-4-(2-phenylethyl)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one.
DR DrugBank; DB07704; 6-AMINO-4-[2-(4-METHOXYPHENYL)ETHYL]-1,7-DIHYDRO-8H-IMIDAZO[4,5-G]QUINAZOLIN-8-ONE.
DR DrugBank; DB08268; 6-AMINO-4-[2-(4-METHYLPHENYL)ETHYL]-1,7-DIHYDRO-8H-IMIDAZO[4,5-G]QUINAZOLIN-8-ONE.
DR DrugBank; DB03074; 7-cyano-7-deazaguanine.
DR DrugBank; DB03304; 7-Deaza-7-Aminomethyl-Guanine.
DR DrugBank; DB02041; Isoluminol.
DR DrugBank; DB14732; Queuine.
DR DrugBank; DB07481; tert-butyl [(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-5-yl)methyl]carbamate.
DR EnsemblBacteria; AAV88987; AAV88987; ZMO0363.
DR KEGG; zmo:ZMO0363; -.
DR eggNOG; COG0343; Bacteria.
DR HOGENOM; CLU_022060_0_1_5; -.
DR OMA; GIDLFDC; -.
DR BRENDA; 2.4.2.29; 6765.
DR BRENDA; 2.4.2.64; 6765.
DR UniPathway; UPA00392; -.
DR EvolutionaryTrace; P28720; -.
DR PRO; PR:P28720; -.
DR Proteomes; UP000001173; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008479; F:queuine tRNA-ribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0101030; P:tRNA-guanine transglycosylation; IEA:InterPro.
DR Gene3D; 3.20.20.105; -; 1.
DR HAMAP; MF_00168; Q_tRNA_Tgt; 1.
DR InterPro; IPR004803; TGT.
DR InterPro; IPR036511; TGT-like_sf.
DR InterPro; IPR002616; tRNA_ribo_trans-like.
DR Pfam; PF01702; TGT; 1.
DR SUPFAM; SSF51713; SSF51713; 1.
DR TIGRFAMs; TIGR00430; Q_tRNA_tgt; 1.
DR TIGRFAMs; TIGR00449; tgt_general; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glycosyltransferase;
KW Metal-binding; Queuosine biosynthesis; Reference proteome; Transferase;
KW tRNA processing; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7665516"
FT CHAIN 2..386
FT /note="Queuine tRNA-ribosyltransferase"
FT /id="PRO_0000135563"
FT REGION 261..267
FT /note="RNA binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168,
FT ECO:0000269|PubMed:12949492"
FT REGION 285..289
FT /note="RNA binding; important for wobble base 34
FT recognition"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168,
FT ECO:0000269|PubMed:12949492"
FT ACT_SITE 102
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168,
FT ECO:0000305|PubMed:12949492"
FT ACT_SITE 280
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168,
FT ECO:0000305|PubMed:12949492"
FT BINDING 102..106
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168,
FT ECO:0000269|PubMed:12949492"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168,
FT ECO:0000269|PubMed:12949492"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168,
FT ECO:0000269|PubMed:12949492"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168,
FT ECO:0000269|PubMed:12949492"
FT BINDING 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168,
FT ECO:0000269|PubMed:10413112, ECO:0000269|PubMed:11178905,
FT ECO:0000269|PubMed:11921407, ECO:0000269|PubMed:12646024,
FT ECO:0000269|PubMed:12909636, ECO:0000269|PubMed:12949492,
FT ECO:0000269|PubMed:14523925, ECO:0000269|PubMed:19627989,
FT ECO:0000269|PubMed:8654383, ECO:0000269|PubMed:8961936"
FT BINDING 320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168,
FT ECO:0000269|PubMed:10413112, ECO:0000269|PubMed:11178905,
FT ECO:0000269|PubMed:11921407, ECO:0000269|PubMed:12646024,
FT ECO:0000269|PubMed:12909636, ECO:0000269|PubMed:12949492,
FT ECO:0000269|PubMed:14523925, ECO:0000269|PubMed:19627989,
FT ECO:0000269|PubMed:8654383, ECO:0000269|PubMed:8961936"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168,
FT ECO:0000269|PubMed:10413112, ECO:0000269|PubMed:11178905,
FT ECO:0000269|PubMed:11921407, ECO:0000269|PubMed:12646024,
FT ECO:0000269|PubMed:12909636, ECO:0000269|PubMed:12949492,
FT ECO:0000269|PubMed:14523925, ECO:0000269|PubMed:19627989,
FT ECO:0000269|PubMed:8654383, ECO:0000269|PubMed:8961936"
FT BINDING 349
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168,
FT ECO:0000269|PubMed:10413112, ECO:0000269|PubMed:11178905,
FT ECO:0000269|PubMed:11921407, ECO:0000269|PubMed:12646024,
FT ECO:0000269|PubMed:12909636, ECO:0000269|PubMed:12949492,
FT ECO:0000269|PubMed:14523925, ECO:0000269|PubMed:19627989,
FT ECO:0000269|PubMed:8654383, ECO:0000269|PubMed:8961936"
FT MUTAGEN 103
FT /note="S->A: Strongly reduces activity."
FT /evidence="ECO:0000269|PubMed:10413112"
FT MUTAGEN 156
FT /note="D->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:8961936"
FT MUTAGEN 280
FT /note="D->N: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:12949492"
FT CONFLICT 312
FT /note="T -> K (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:7A4K"
FT STRAND 13..22
FT /evidence="ECO:0007829|PDB:5N6F"
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:5N6F"
FT STRAND 35..43
FT /evidence="ECO:0007829|PDB:5N6F"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:6YGW"
FT HELIX 56..61
FT /evidence="ECO:0007829|PDB:5N6F"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:5I03"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:5N6F"
FT HELIX 71..76
FT /evidence="ECO:0007829|PDB:5N6F"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:2POT"
FT HELIX 80..85
FT /evidence="ECO:0007829|PDB:5N6F"
FT HELIX 89..93
FT /evidence="ECO:0007829|PDB:5N6F"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:5N6F"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:5N6F"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:1EFZ"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:6YGW"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:5N6F"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:6YYZ"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:5N6F"
FT HELIX 137..147
FT /evidence="ECO:0007829|PDB:5N6F"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:5N6F"
FT HELIX 165..188
FT /evidence="ECO:0007829|PDB:5N6F"
FT HELIX 190..195
FT /evidence="ECO:0007829|PDB:5N6F"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:5N6F"
FT HELIX 208..221
FT /evidence="ECO:0007829|PDB:5N6F"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:5N6F"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:4Q8W"
FT HELIX 237..247
FT /evidence="ECO:0007829|PDB:5N6F"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:5N6F"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:1P0E"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:5N6F"
FT HELIX 265..272
FT /evidence="ECO:0007829|PDB:5N6F"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:5N6F"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:5N6F"
FT HELIX 283..290
FT /evidence="ECO:0007829|PDB:5N6F"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:5LPS"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:5LPS"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:5N6F"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:4Q8W"
FT HELIX 321..325
FT /evidence="ECO:0007829|PDB:5N6F"
FT HELIX 328..336
FT /evidence="ECO:0007829|PDB:5N6F"
FT HELIX 340..366
FT /evidence="ECO:0007829|PDB:5N6F"
FT HELIX 370..383
FT /evidence="ECO:0007829|PDB:5N6F"
SQ 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
