ID A0A0G0MY72_9BACT Unreviewed; 378 AA. AC A0A0G0MY72; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 24-JUL-2024, entry version 39. 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 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 large RT radiation of phyla."; RL Nature 0:0-0(2015). 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 AlphaFoldDB; A0A0G0MY72; -. DR STRING; 1619067.UT36_C0003G0034; -. DR PATRIC; fig|1619067.4.peg.347; -. DR UniPathway; UPA00392; -. DR Proteomes; UP000034818; Unassembled WGS sequence. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008479; F:tRNA-guanosine(34) queuine transglycosylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0002099; P:tRNA wobble guanine modification; IEA:TreeGrafter. 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; IPR050076; ArchSynthase1/Queuine_TRR. DR InterPro; IPR004803; TGT. DR InterPro; IPR036511; TGT-like_sf. DR InterPro; IPR002616; tRNA_ribo_trans-like. DR NCBIfam; TIGR00430; Q_tRNA_tgt; 1. DR NCBIfam; TIGR00449; tgt_general; 1. 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. 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|HAMAP-Rule:MF_00168}; 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..374 FT /note="tRNA-guanine(15) transglycosylase-like" FT /evidence="ECO:0000259|Pfam:PF01702" FT REGION 254..260 FT /note="RNA binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168" FT REGION 278..282 FT /note="RNA binding; important for wobble base 34 FT recognition" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168" FT ACT_SITE 90 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168" FT ACT_SITE 273 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168" FT BINDING 90..94 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168" FT BINDING 144 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168" FT BINDING 196 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168" FT BINDING 223 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168" FT BINDING 311 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168" FT BINDING 313 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168" FT BINDING 316 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168" FT BINDING 342 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="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 //