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 27-MAR-2024, entry version 186. 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; Pseudomonadota; 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00168, ECO:0000269|PubMed:10413112, CC ECO:0000269|PubMed:11178905, ECO:0000269|PubMed:11921407, CC ECO:0000269|PubMed:12646024, ECO:0000269|PubMed:12909636, CC ECO:0000269|PubMed:12949492, ECO:0000269|PubMed:14523925, CC ECO:0000269|PubMed:19627989, ECO:0000269|PubMed:8654383, CC 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 RefSeq; WP_023593392.1; NC_022900.1. 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 GeneID; 79904432; -. DR KEGG; zmo:ZMO0363; -. DR eggNOG; COG0343; Bacteria. DR HOGENOM; CLU_022060_0_1_5; -. 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:tRNA-guanosine(34) queuine transglycosylase 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; Queuine tRNA-ribosyltransferase-like; 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 NCBIfam; TIGR00430; Q_tRNA_tgt; 1. DR NCBIfam; TIGR00449; tgt_general; 1. DR PANTHER; PTHR46499; QUEUINE TRNA-RIBOSYLTRANSFERASE; 1. DR PANTHER; PTHR46499:SF1; QUEUINE TRNA-RIBOSYLTRANSFERASE; 1. DR Pfam; PF01702; TGT; 1. DR SUPFAM; SSF51713; tRNA-guanine transglycosylase; 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 //