ID D2NPM3_ROTMD Unreviewed; 466 AA. AC D2NPM3; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 02-NOV-2016, entry version 53. DE RecName: Full=Queuine tRNA-ribosyltransferase {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00087750}; DE EC=2.4.2.29 {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00087822}; 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; Actinobacteria; Micrococcales; Micrococcaceae; Rothia. OX NCBI_TaxID=680646 {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. CC -!- FUNCTION: Catalyzes the base-exchange of a guanine (G) residue CC with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at CC position 34 (anticodon wobble position) in tRNAs with GU(N) CC anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs CC through a double-displacement mechanism. The nucleophile active CC site attacks the C1' of nucleotide 34 to detach the guanine base CC from the RNA, forming a covalent enzyme-RNA intermediate. The CC proton acceptor active site deprotonates the incoming PreQ1, CC allowing a nucleophilic attack on the C1' of the ribose to form CC the product. After dissociation, two additional enzymatic CC reactions on the tRNA convert PreQ1 to queuine (Q), resulting in CC the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2- CC cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). CC {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777, CC ECO:0000256|SAAS:SAAS00628203}. CC -!- CATALYTIC ACTIVITY: Guanine(34) in tRNA + 7-aminomethyl-7- CC carbaguanine = 7-aminomethyl-7-carbaguanine(34) in tRNA + guanine. CC {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777, CC ECO:0000256|SAAS:SAAS00087626}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|RuleBase:RU003777}; CC Note=Binds 1 zinc ion per subunit. CC {ECO:0000256|RuleBase:RU003777}; CC -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|SAAS:SAAS00087869}. CC -!- SUBUNIT: Homodimer. Within each dimer, one monomer is responsible CC for RNA recognition and catalysis, while the other monomer binds CC to the replacement base PreQ1. {ECO:0000256|SAAS:SAAS00628204}. CC -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family. CC {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777, CC ECO:0000256|SAAS:SAAS00571098}. 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 STRING; 680646.RMDY18_17590; -. DR EnsemblBacteria; BAI65591; BAI65591; RMDY18_17590. DR KEGG; rmu:RMDY18_17590; -. DR PATRIC; 35273999; VBIRotMuc152186_1520. DR eggNOG; ENOG4105C6U; Bacteria. DR eggNOG; COG0343; LUCA. DR HOGENOM; HOG000223473; -. DR KO; K00773; -. DR OMA; GIDLFDC; -. DR UniPathway; UPA00392; -. DR Proteomes; UP000001883; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008479; F:queuine tRNA-ribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006400; P:tRNA modification; IEA:InterPro. DR Gene3D; 3.20.20.105; -; 2. DR HAMAP; MF_00168; Q_tRNA_Tgt; 1. DR InterPro; IPR004803; Queuine_tRNA-ribosylTrfase. DR InterPro; IPR002616; tRNA_ribo_trans-like. DR Pfam; PF01702; TGT; 1. DR SUPFAM; SSF51713; SSF51713; 2. DR TIGRFAMs; TIGR00430; Q_tRNA_tgt; 1. DR TIGRFAMs; TIGR00449; tgt_general; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001883}; KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00168, KW ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00460875}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00168, KW ECO:0000256|SAAS:SAAS00460860}; KW Queuosine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00168, KW ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00460855}; KW Reference proteome {ECO:0000313|Proteomes:UP000001883}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00168, KW ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00460853, KW ECO:0000313|EMBL:BAI65591.1}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_00168, KW ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00460804}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777, KW ECO:0000256|SAAS:SAAS00460797}. FT REGION 148 152 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00168}. FT REGION 364 368 RNA binding; important for wobble base 34 FT recognition. {ECO:0000256|HAMAP-Rule: FT MF_00168}. FT ACT_SITE 148 148 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_00168}. FT ACT_SITE 359 359 Nucleophile. {ECO:0000256|HAMAP-Rule: FT MF_00168}. FT METAL 397 397 Zinc. {ECO:0000256|HAMAP-Rule:MF_00168}. FT METAL 399 399 Zinc. {ECO:0000256|HAMAP-Rule:MF_00168}. FT METAL 402 402 Zinc. {ECO:0000256|HAMAP-Rule:MF_00168}. FT METAL 428 428 Zinc; via pros nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00168}. FT BINDING 235 235 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00168}. FT BINDING 285 285 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00168}. FT BINDING 312 312 Substrate; via amide nitrogen. FT {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 //