ID TGT_CAMFF Reviewed; 374 AA. AC A0RPL5; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 1. DT 02-SEP-2026, entry version 101. 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}; GN OrderedLocusNames=CFF8240_0980; OS Campylobacter fetus subsp. fetus (strain 82-40). OC Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria; OC Campylobacterales; Campylobacteraceae; Campylobacter. OX NCBI_TaxID=360106; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=82-40; RA Fouts D.E., Nelson K.E.; RT "Sequence of Campylobacter fetus subsp. fetus 82-40."; RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases. 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 -!- 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}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00168}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00168}; CC -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00168}. 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 -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family. CC {ECO:0000255|HAMAP-Rule:MF_00168}. 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; CP000487; ABK81825.1; -; Genomic_DNA. DR RefSeq; WP_002849532.1; NC_008599.1. DR AlphaFoldDB; A0RPL5; -. DR SMR; A0RPL5; -. DR GeneID; 61064810; -. DR KEGG; cff:CFF8240_0980; -. DR eggNOG; COG0343; Bacteria. DR HOGENOM; CLU_022060_0_1_7; -. DR UniPathway; UPA00392; -. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0008479; F:tRNA-guanosine(34) queuine transglycosylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008616; P:tRNA queuosine(34) biosynthetic process; IEA:UniProtKB-UniRule. 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; PTHR43530; QUEUINE TRNA-RIBOSYLTRANSFERASE CATALYTIC SUBUNIT 1; 1. DR PANTHER; PTHR43530:SF1; QUEUINE TRNA-RIBOSYLTRANSFERASE CATALYTIC SUBUNIT 1; 1. DR Pfam; PF01702; TGT; 1. DR SUPFAM; SSF51713; tRNA-guanine transglycosylase; 1. PE 3: Inferred from homology; KW Glycosyltransferase; Metal-binding; Queuosine biosynthesis; Transferase; KW tRNA processing; Zinc. FT CHAIN 1..374 FT /note="Queuine tRNA-ribosyltransferase" FT /id="PRO_1000016769" FT REGION 251..257 FT /note="RNA binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168" FT REGION 275..279 FT /note="RNA binding; important for wobble base 34 FT recognition" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168" FT ACT_SITE 90 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168" FT ACT_SITE 270 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168" FT BINDING 90..94 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168" FT BINDING 144 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168" FT BINDING 193 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168" FT BINDING 220 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168" FT BINDING 308 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168" FT BINDING 310 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168" FT BINDING 313 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168" FT BINDING 339 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168" SQ SEQUENCE 374 AA; 42297 MW; 0A48196FCBAEE4EB CRC64; MNFKIDKTDG NARACTLQTA HSTIQTPIFM PVGTLGAVKS LDAIDLKEIL DAKIILANTY HLYLRPTSKV VREFGGLHGF SKFDRSFLTD SGGFQAFSLS KISKPDENGI KFKSHIDGSM HYFTPKSVLD TQYDLSSDIM MILDDLVALP ATKERIDLSI KRTINWAKIA CEYHKSNKQK SVGIDQNIFG IIQGGTDYNA RKLCAEALCE MEFDGLAIGG LSVGESNEEM YDTVEALMPF IDKNRPRYLM GVGTPEDLVQ NVERGVDMFD CVMPTRNARN GTLFTSFGKI NIKSAAFIKD DNKIDPECDC YTCSNFSRGY LNHLYKAREL TFFRLASLHN LHYYLNLVKQ MREAIMQGKF KEFKREFYAK RGMI //