ID A0A078KB76_9GAMM Unreviewed; 363 AA. AC A0A078KB76; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 04-MAR-2015, entry version 4. 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 ECO:0000313|EMBL:CDZ16426.1}; GN ORFNames=CEM_159 {ECO:0000313|EMBL:CDZ16426.1}; OS Candidatus Evansia muelleri. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Zymobacter group; Candidatus Evansia. OX NCBI_TaxID=1495769 {ECO:0000313|EMBL:CDZ16426.1}; RN [1] {ECO:0000313|EMBL:CDZ16426.1} RP NUCLEOTIDE SEQUENCE. RA Santos-Garcia Diego; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. 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). CC {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777, CC ECO:0000256|SAAS:SAAS00087893}. 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 ECO:0000256|SAAS:SAAS00173048}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00168, ECO:0000256|RuleBase:RU003777, CC ECO:0000256|SAAS:SAAS00173048}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 1 zinc ion per subunit.; CC -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|SAAS:SAAS00087869}. CC -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis. CC -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family. CC {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777}. 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; LM655252; CDZ16426.1; -; Genomic_DNA. DR UniPathway; UPA00392; -. 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 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 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 89 89 Nucleophile. {ECO:0000256|HAMAP-Rule: FT MF_00168}. FT METAL 298 298 Zinc. {ECO:0000256|HAMAP-Rule:MF_00168}. FT METAL 300 300 Zinc. {ECO:0000256|HAMAP-Rule:MF_00168}. FT METAL 303 303 Zinc. {ECO:0000256|HAMAP-Rule:MF_00168}. FT METAL 329 329 Zinc. {ECO:0000256|HAMAP-Rule:MF_00168}. FT BINDING 90 90 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00168}. SQ SEQUENCE 363 AA; 41532 MW; 291583EEDA9C6C80 CRC64; MRFRLLSKIG RARYGQLIFN RGIVDTPNFI PVGTYGAIKG LNHDDLNAGG VEIILSNTFH LLLRPGLNSI IKHGGLHNFI QWKKPILTDS GGFQVFSFVN MIKIIEEGVY FNINGKNIFI GPEESVLIQR ILGSDIIMIF DYCPPYPMTY KNAKTSMELS LRWAKRSHYA HVGSRSALFG IIQGSIYRKL RERSLLGLMD IGFDGLAIGG LSVGEPKQEM IKVLNYLPML MPDNKPRYLM GVGKPEDLVE GVCRGIDIFD CVIPTRNARN GHLYTFKGII NIRNSKHKHS NFTVEKYCDC YTCKYFSRSY LHHLYHCKDI LGAKLNTIHN IRYYQRLMAN LRNAIKNGTL DYFVSDFYKC RMH //