ID A0A0G0MY72_9BACT Unreviewed; 378 AA. AC A0A0G0MY72; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 16-SEP-2015, entry version 2. DE RecName: Full=Queuine tRNA-ribosyltransferase {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777}; DE EC=2.4.2.29 {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777}; 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 Peregrinibacteria bacterium GW2011_GWF2_39_17. OC Bacteria; Peregrinibacteria. OX NCBI_TaxID=1619067 {ECO:0000313|EMBL:KKR08914.1, ECO:0000313|Proteomes:UP000034818}; RN [1] {ECO:0000313|EMBL:KKR08914.1} RP NUCLEOTIDE SEQUENCE. 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: Exchanges the guanine residue with 7-aminomethyl-7- CC deazaguanine in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His CC and -Tyr). After this exchange, a cyclopentendiol moiety is CC attached to the 7-aminomethyl group of 7-deazaguanine, resulting CC in the hypermodified nucleoside queuosine (Q) (7-(((4,5-cis- CC dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine) (By CC similarity). {ECO:0000256|SAAS:SAAS00206996}. 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 -!- CATALYTIC ACTIVITY: Guanine(34) in tRNA + queuine = queuosine(34) CC in tRNA + guanine. {ECO:0000256|HAMAP-Rule:MF_00168, CC ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00087703}. 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 -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family. CC {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777}. 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 UniPathway; UPA00392; -. DR Proteomes; UP000034818; Unassembled WGS sequence. DR GO; GO:0008479; F:queuine tRNA-ribosyltransferase activity; IEA:UniProtKB-EC. DR Gene3D; 3.20.20.105; -; 1. DR HAMAP; MF_00168; Q_tRNA_Tgt; 1. DR InterPro; IPR004803; Queuine_tRNA-ribosylTrfase. DR InterPro; IPR002616; tRNA_ribo_trans-like. DR PANTHER; PTHR11962; PTHR11962; 1. 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}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00168, KW ECO:0000256|SAAS:SAAS00087792}; KW Queuosine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00168, KW ECO:0000256|RuleBase:RU003777}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00168, KW ECO:0000256|RuleBase:RU003777}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_00168, KW ECO:0000256|RuleBase:RU003777}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777}. FT ACT_SITE 90 90 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. {ECO:0000256|HAMAP-Rule:MF_00168}. FT BINDING 91 91 Substrate. {ECO:0000256|HAMAP-Rule: FT 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 //