ID A0A078KB76_9GAMM Unreviewed; 363 AA. AC A0A078KB76; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 28-MAR-2018, entry version 27. DE RecName: Full=Queuine tRNA-ribosyltransferase {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00102053}; DE EC=2.4.2.29 {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00384033}; 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, ECO:0000313|Proteomes:UP000032420}; 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: 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:SAAS00102009}. 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:SAAS00384008}. 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:SAAS01002254}. 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 RefSeq; WP_045086208.1; NZ_LM655252.1. DR EnsemblBacteria; CDZ16426; CDZ16426; CEM_159. DR KEGG; eme:CEM_159; -. DR PATRIC; fig|1495769.3.peg.148; -. DR KO; K00773; -. DR UniPathway; UPA00392; -. DR Proteomes; UP000032420; Chromosome. 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:UP000032420}; KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00168, KW ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS01002259, KW ECO:0000313|EMBL:CDZ16426.1}; 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|SAAS:SAAS00087839}; KW Reference proteome {ECO:0000313|Proteomes:UP000032420}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00168, KW ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00876991, KW ECO:0000313|EMBL:CDZ16426.1}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_00168, KW ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00087682}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777, KW ECO:0000256|SAAS:SAAS00460797}. FT DOMAIN 125 357 TGT. {ECO:0000259|Pfam:PF01702}. FT REGION 89 93 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00168}. FT REGION 241 247 RNA binding. {ECO:0000256|HAMAP-Rule: FT MF_00168}. FT REGION 265 269 RNA binding; important for wobble base 34 FT recognition. {ECO:0000256|HAMAP-Rule: FT MF_00168}. FT ACT_SITE 89 89 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_00168}. FT ACT_SITE 260 260 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; via pros nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00168}. FT BINDING 141 141 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00168}. FT BINDING 183 183 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00168}. FT BINDING 210 210 Substrate; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule: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 //