ID A0A078KB76_9GAMM Unreviewed; 363 AA. AC A0A078KB76; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 22-FEB-2023, entry version 42. DE RecName: Full=Queuine tRNA-ribosyltransferase {ECO:0000256|HAMAP-Rule:MF_00168}; DE EC=2.4.2.29 {ECO:0000256|HAMAP-Rule:MF_00168}; 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|Proteomes:UP000032420} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Santos-Garcia D.; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the base-exchange of a guanine (G) residue with the CC queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 CC (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, CC -Asn, -His and -Tyr). Catalysis occurs through a double-displacement CC mechanism. The nucleophile active site attacks the C1' of nucleotide 34 CC to detach the guanine base from the RNA, forming a covalent enzyme-RNA CC intermediate. The proton acceptor active site deprotonates the incoming CC PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form CC the product. After dissociation, two additional enzymatic reactions on CC the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified CC nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1- CC yl)amino)methyl)-7-deazaguanosine). {ECO:0000256|HAMAP-Rule:MF_00168}. 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-COMP:10342, CC ChEBI:CHEBI:16235, ChEBI:CHEBI:58703, ChEBI:CHEBI:74269, CC ChEBI:CHEBI:82833; EC=2.4.2.29; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00168}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00168}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00168}; CC -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_00168}. CC -!- SUBUNIT: Homodimer. Within each dimer, one monomer is responsible for CC RNA recognition and catalysis, while the other monomer binds to the CC replacement base PreQ1. {ECO:0000256|HAMAP-Rule:MF_00168}. CC -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family. CC {ECO:0000256|HAMAP-Rule:MF_00168}. 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 AlphaFoldDB; A0A078KB76; -. DR STRING; 1495769.CEM_159; -. DR KEGG; eme:CEM_159; -. DR PATRIC; fig|1495769.3.peg.148; -. DR HOGENOM; CLU_022060_0_1_6; -. DR OrthoDB; 9805417at2; -. 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; Queuine tRNA-ribosyltransferase-like; 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 PANTHER; PTHR46499; QUEUINE TRNA-RIBOSYLTRANSFERASE; 1. DR PANTHER; PTHR46499:SF1; QUEUINE TRNA-RIBOSYLTRANSFERASE; 1. DR Pfam; PF01702; TGT; 1. DR SUPFAM; SSF51713; tRNA-guanine transglycosylase; 1. DR TIGRFAMs; TIGR00430; Q_tRNA_tgt; 1. DR TIGRFAMs; TIGR00449; tgt_general; 1. PE 3: Inferred from homology; KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP- KW Rule:MF_00168}; Metal-binding {ECO:0000256|HAMAP-Rule:MF_00168}; KW Queuosine biosynthesis {ECO:0000256|ARBA:ARBA00022785, ECO:0000256|HAMAP- KW Rule:MF_00168}; Reference proteome {ECO:0000313|Proteomes:UP000032420}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00168}; KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP- KW Rule:MF_00168}; Zinc {ECO:0000256|HAMAP-Rule:MF_00168}. FT DOMAIN 12..359 FT /note="tRNA-guanine(15) transglycosylase-like" FT /evidence="ECO:0000259|Pfam:PF01702" FT REGION 241..247 FT /note="RNA binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168" FT REGION 265..269 FT /note="RNA binding; important for wobble base 34 FT recognition" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168" FT ACT_SITE 89 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168" FT ACT_SITE 260 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168" FT BINDING 89..93 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168" FT BINDING 141 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168" FT BINDING 183 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168" FT BINDING 210 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168" FT BINDING 298 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168" FT BINDING 300 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168" FT BINDING 303 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168" FT BINDING 329 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="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 //