ID TGT_RICCN Reviewed; 361 AA. AC Q92GM6; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 110. 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=RC1097; OS Rickettsia conorii (strain ATCC VR-613 / Malish 7). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=272944; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-613 / Malish 7; RX PubMed=11557893; DOI=10.1126/science.1061471; RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.; RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii."; RL Science 293:2093-2098(2001). 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; AE006914; AAL03635.1; -; Genomic_DNA. DR PIR; A97837; A97837. DR RefSeq; WP_004997587.1; NC_003103.1. DR AlphaFoldDB; Q92GM6; -. DR SMR; Q92GM6; -. DR GeneID; 928246; -. DR KEGG; rco:RC1097; -. DR HOGENOM; CLU_022060_0_1_5; -. DR UniPathway; UPA00392; -. DR Proteomes; UP000000816; 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 3: Inferred from homology; KW Glycosyltransferase; Metal-binding; Queuosine biosynthesis; Transferase; KW tRNA processing; Zinc. FT CHAIN 1..361 FT /note="Queuine tRNA-ribosyltransferase" FT /id="PRO_0000135513" FT REGION 247..253 FT /note="RNA binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168" FT REGION 271..275 FT /note="RNA binding; important for wobble base 34 FT recognition" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168" FT ACT_SITE 92 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168" FT ACT_SITE 266 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168" FT BINDING 92..96 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168" FT BINDING 146 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168" FT BINDING 189 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168" FT BINDING 216 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168" FT BINDING 304 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168" FT BINDING 306 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168" FT BINDING 309 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168" FT BINDING 335 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168" SQ SEQUENCE 361 AA; 40590 MW; 1BEC5C2C39341A84 CRC64; MSKFSFNIHH QHKKARSGII VTAHGEMRTP AFMPVGTRGT VKAMLPESVA ETGADILLGN TYHLMLQPTA ERIVQLGGLH KFMNWDKPIL TDSGGFQVMS LSKLCKITEE GVSFSSHING DKYMLTPERS TEIQYLLGST ITMAFDECTP YPATFEEAKT SMQLTTRWAN RSRNAFVKRE GYAQFGIIQG SVYEELREQS AKDLVELDFE GYAIGGLAVG EGQELMFKVL DYAPEFLPQN KPRYLMGVGK PVDIIGAVSR GIDMFDCVIP TRSGRNGQAF TKYGTVNIRN SKYADDNKPL EHDCLCPACR NYSKAYLHHL VRIGEILGSM LMTWHNLTYF QNLMSRIRAY IKLGKDFDFD S //