ID A0A0G0MY72_9BACT Unreviewed; 378 AA. AC A0A0G0MY72; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 08-MAY-2019, entry version 24. 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 ORFNames=UT36_C0003G0034 {ECO:0000313|EMBL:KKR08914.1}; OS Candidatus Peregrinibacteria bacterium GW2011_GWF2_39_17. OC Bacteria; Candidatus Peregrinibacteria. OX NCBI_TaxID=1619067 {ECO:0000313|EMBL:KKR08914.1, ECO:0000313|Proteomes:UP000034818}; RN [1] {ECO:0000313|EMBL:KKR08914.1, ECO:0000313|Proteomes:UP000034818} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A., RA Wilkins M.J., Williams K.H., Banfield J.F.; RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a RT large radiation of phyla."; RL Nature 0:0-0(2015). 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: 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- CC COMP:10342, ChEBI:CHEBI:16235, ChEBI:CHEBI:58703, CC ChEBI:CHEBI:74269, ChEBI:CHEBI:82833; EC=2.4.2.29; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00168, CC ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS01115764}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00168, ECO:0000256|RuleBase:RU003777}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00168, 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|HAMAP-Rule:MF_00168, CC 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKR08914.1}. 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; LBWM01000003; KKR08914.1; -; Genomic_DNA. DR EnsemblBacteria; KKR08914; KKR08914; UT36_C0003G0034. DR PATRIC; fig|1619067.4.peg.347; -. DR UniPathway; UPA00392; -. DR Proteomes; UP000034818; Unassembled WGS sequence. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008479; F:queuine tRNA-ribosyltransferase 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; -; 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 Pfam; PF01702; TGT; 1. DR SUPFAM; SSF51713; SSF51713; 1. DR TIGRFAMs; TIGR00430; Q_tRNA_tgt; 1. DR TIGRFAMs; TIGR00449; tgt_general; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000034818}; KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00168, KW ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00460875, KW ECO:0000313|EMBL:KKR08914.1}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00168, KW ECO:0000256|SAAS:SAAS00101950}; KW Queuosine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00168, KW ECO:0000256|SAAS:SAAS00460855}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00168, KW ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00876991, KW ECO:0000313|EMBL:KKR08914.1}; 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:SAAS00087669}. FT DOMAIN 12 373 TGT. {ECO:0000259|Pfam:PF01702}. FT REGION 90 94 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00168}. FT REGION 254 260 RNA binding. {ECO:0000256|HAMAP-Rule: FT MF_00168}. FT REGION 278 282 RNA binding; important for wobble base 34 FT recognition. {ECO:0000256|HAMAP-Rule: FT MF_00168}. FT ACT_SITE 90 90 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_00168}. FT ACT_SITE 273 273 Nucleophile. {ECO:0000256|HAMAP-Rule: FT MF_00168}. FT METAL 311 311 Zinc. {ECO:0000256|HAMAP-Rule:MF_00168}. FT METAL 313 313 Zinc. {ECO:0000256|HAMAP-Rule:MF_00168}. FT METAL 316 316 Zinc. {ECO:0000256|HAMAP-Rule:MF_00168}. FT METAL 342 342 Zinc; via pros nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00168}. FT BINDING 144 144 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00168}. FT BINDING 196 196 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00168}. FT BINDING 223 223 Substrate; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00168}. SQ SEQUENCE 378 AA; 43207 MW; 45EBC6750811FCB1 CRC64; MFTFKINHTN DRARLGQYFT PHGIINTPAF IPCGTKGVVK TLEIRDLHDL GVEIMLSNTY HLTIRPGAEA IKKWEGLHRW MGWDKPLLTD SGGFQVFSLN ATRKIDDQGV EFKSPLNGTR HYFTPESVMQ IQEKLGADII MAFDECADGN SDKAYAKKAM ERTHKWAKQC QKENSKLQKL RALNGQFPQA LFPIIQGVIY EDLRIESTKF MADLDLPGIA IGGLSVGEKK EDMYRVLDII YPHLPNDKIH YLMGVGSPED LVEGVARGID LFDCVLPTRL ARHGAFWTET GRYNIKNKKF EQELMPLAEN CTCSTCKSCS CSYIRHLFME KEITALRLLS IHNLHFLLTL VHEIRVQIGK GNFENFRQEF HNQFLNLK //