ID D2NPM3_ROTMD Unreviewed; 466 AA. AC D2NPM3; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 29-MAY-2024, entry version 88. DE RecName: Full=Queuine tRNA-ribosyltransferase {ECO:0000256|HAMAP-Rule:MF_00168}; DE EC=2.4.2.29 {ECO:0000256|HAMAP-Rule:MF_00168}; DE AltName: Full=Guanine insertion enzyme {ECO:0000256|HAMAP-Rule:MF_00168}; DE AltName: Full=tRNA-guanine transglycosylase {ECO:0000256|HAMAP-Rule:MF_00168}; GN Name=tgt {ECO:0000256|HAMAP-Rule:MF_00168}; GN OrderedLocusNames=RMDY18_17590 {ECO:0000313|EMBL:BAI65591.1}; OS Rothia mucilaginosa (strain DY-18) (Stomatococcus mucilaginosus). OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae; OC Rothia. OX NCBI_TaxID=680646 {ECO:0000313|EMBL:BAI65591.1, ECO:0000313|Proteomes:UP000001883}; RN [1] {ECO:0000313|Proteomes:UP000001883} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DY-18 {ECO:0000313|Proteomes:UP000001883}; RA Yamane K., Nambu T., Mashimo C., Sugimori C., Yamanaka T., Leung K., RA Fukushima H.; RT "Complete genome sequence of Rothia mucilaginosa DJ."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:BAI65591.1, ECO:0000313|Proteomes:UP000001883} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DY-18 {ECO:0000313|EMBL:BAI65591.1, RC ECO:0000313|Proteomes:UP000001883}; RA Yamane K., Yoshida M., Fujihira T., Baba T., Tsuji N., Hayashi H., RA Sugimori C., Yamanaka T., Mashimo C., Nambu T., Kawai H., Fukushima H.; RT "Isolation and identification of Rothia mucilaginosa from persistent apical RT periodontitis lesions."; RL J Osaka Dent Univ 44:93-98(2010). RN [3] {ECO:0000313|EMBL:BAI65591.1, ECO:0000313|Proteomes:UP000001883} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DY-18 {ECO:0000313|EMBL:BAI65591.1, RC ECO:0000313|Proteomes:UP000001883}; RA Yamane K., Nambu T., Yamanaka T., Mashimo C., Sugimori C., Leung K.-P., RA Fukushima H.; RT "Complete Genome Sequence of Rothia mucilaginosa DY-18: A Clinical Isolate RT with Dense Meshwork-Like Structures from a Persistent Apical Periodontitis RT Lesion."; RL Sequencing 2010:457236-457236(2010). 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:0000256|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:0000256|HAMAP- CC Rule:MF_00168}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00168}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00168}; CC -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis. CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_00168}. CC -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family. CC {ECO:0000256|HAMAP-Rule:MF_00168}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|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; AP011540; BAI65591.1; -; Genomic_DNA. DR AlphaFoldDB; D2NPM3; -. DR STRING; 680646.RMDY18_17590; -. DR KEGG; rmu:RMDY18_17590; -. DR eggNOG; COG0343; Bacteria. DR HOGENOM; CLU_022060_0_0_11; -. DR UniPathway; UPA00392; -. DR Proteomes; UP000001883; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. 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:0002099; P:tRNA wobble guanine modification; IEA:TreeGrafter. 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; 2. DR SUPFAM; SSF51713; tRNA-guanine transglycosylase; 1. PE 3: Inferred from homology; KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP- KW Rule:MF_00168}; Metal-binding {ECO:0000256|HAMAP-Rule:MF_00168}; KW Queuosine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00168}; KW Reference proteome {ECO:0000313|Proteomes:UP000001883}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00168}; KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP- KW Rule:MF_00168}; Zinc {ECO:0000256|HAMAP-Rule:MF_00168}. FT DOMAIN 71..158 FT /note="tRNA-guanine(15) transglycosylase-like" FT /evidence="ECO:0000259|Pfam:PF01702" FT DOMAIN 193..461 FT /note="tRNA-guanine(15) transglycosylase-like" FT /evidence="ECO:0000259|Pfam:PF01702" FT REGION 1..20 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 364..368 FT /note="RNA binding; important for wobble base 34 FT recognition" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168" FT ACT_SITE 148 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168" FT ACT_SITE 359 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168" FT BINDING 148..152 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168" FT BINDING 235 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168" FT BINDING 285 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168" FT BINDING 312 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168" FT BINDING 397 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168" FT BINDING 399 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168" FT BINDING 402 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168" FT BINDING 428 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168" SQ SEQUENCE 466 AA; 51371 MW; D80AECC5B94CCDA7 CRC64; MRTPPPAKEA GFSGRLGCRH SDGKQTIERR MSVLDNSFPT EDFGFTITSR LADTASPSAE RVEANGGQFR GRTGVITTPH GQIQTPAFTP VGTKATVKAV LPESMKELGA QALLSNAYHL YLQPGPEILD AAGGLGAFMN WDGPTFTDSG GFQVMSLGSG FKKVIDMGTV ADAKGADGRP LGDDDVAKGK ERLAHIDDDG VNFKSHIDGS IHRFTPEVSM QVQHQIGADV MFAFDELTTL YNSRGYQEEA LERTRLWALR CIAEHQRLTA ERVGKPYQAL FGVIQGAQYE DLRRKACQDL GSMPFDGFGI GGALEKENLG TIVRWCAEEL PESKPRHLLG ISEPDDIFVG IENGVDTFDC VSPTRVARNA AVYSPTGRYN ITNARFKADF SPIYEGCDCY TCTHYTRAYL RHLFKADERL AATLASIHNE RFIVRMVDDA REAIKDGTYF EYRDEFLGNY YSGKKP //