ID B2RAR3_HUMAN Unreviewed; 403 AA. AC B2RAR3; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 29-MAY-2024, entry version 82. DE RecName: Full=Queuine tRNA-ribosyltransferase catalytic subunit 1 {ECO:0000256|HAMAP-Rule:MF_03218}; DE EC=2.4.2.64 {ECO:0000256|HAMAP-Rule:MF_03218}; DE AltName: Full=Guanine insertion enzyme {ECO:0000256|HAMAP-Rule:MF_03218}; DE AltName: Full=tRNA-guanine transglycosylase {ECO:0000256|HAMAP-Rule:MF_03218}; GN Name=QTRT1 {ECO:0000256|HAMAP-Rule:MF_03218}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG36960.1}; RN [1] {ECO:0000313|EMBL:BAG36960.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Amygdala {ECO:0000313|EMBL:BAG36960.1}; RA Wakamatsu A., Yamamoto J., Kimura K., Kaida T., Tsuchiya K., Iida Y., RA Takayama Y., Murakawa K., Kanehori K., Andoh T., Kagawa N., Sato R., RA Kawamura Y., Tanaka S., Kisu Y., Sugano S., Goshima N., Nomura N., RA Isogai T.; RT "NEDO functional analysis of protein and research application project."; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalytic subunit of the queuine tRNA-ribosyltransferase CC (TGT) that catalyzes the base-exchange of a guanine (G) residue with CC queuine (Q) at position 34 (anticodon wobble position) in tRNAs with CC GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the CC hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2- CC cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). Catalysis occurs CC through a double-displacement mechanism. The nucleophile active site CC attacks the C1' of nucleotide 34 to detach the guanine base from the CC RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor CC active site deprotonates the incoming queuine, allowing a nucleophilic CC attack on the C1' of the ribose to form the product. CC {ECO:0000256|HAMAP-Rule:MF_03218}. CC -!- CATALYTIC ACTIVITY: CC Reaction=guanosine(34) in tRNA + queuine = guanine + queuosine(34) in CC tRNA; Xref=Rhea:RHEA:16633, Rhea:RHEA-COMP:10341, Rhea:RHEA- CC COMP:18571, ChEBI:CHEBI:16235, ChEBI:CHEBI:17433, ChEBI:CHEBI:74269, CC ChEBI:CHEBI:194431; EC=2.4.2.64; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03218}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03218}; CC -!- SUBUNIT: Heterodimer of a catalytic subunit QTRT1 and an accessory CC subunit QTRT2. {ECO:0000256|HAMAP-Rule:MF_03218}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03218}. CC Mitochondrion outer membrane {ECO:0000256|HAMAP-Rule:MF_03218}; CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_03218}; CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_03218}. Note=Weakly CC associates with mitochondria, possibly via QTRT2. {ECO:0000256|HAMAP- CC Rule:MF_03218}. CC -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family. CC {ECO:0000256|HAMAP-Rule:MF_03218}. 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; AK314308; BAG36960.1; -; mRNA. DR AlphaFoldDB; B2RAR3; -. DR PeptideAtlas; B2RAR3; -. DR ChiTaRS; QTRT1; human. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell. 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:0101030; P:tRNA-guanine transglycosylation; IEA:UniProtKB-UniRule. 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 NCBIfam; TIGR00430; Q_tRNA_tgt; 1. DR NCBIfam; TIGR00449; tgt_general; 1. DR PANTHER; PTHR43530; QUEUINE TRNA-RIBOSYLTRANSFERASE CATALYTIC SUBUNIT 1; 1. DR PANTHER; PTHR43530:SF1; QUEUINE TRNA-RIBOSYLTRANSFERASE CATALYTIC SUBUNIT 1; 1. DR Pfam; PF01702; TGT; 1. DR SUPFAM; SSF51713; tRNA-guanine transglycosylase; 1. PE 2: Evidence at transcript level; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03218}; KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_03218}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_03218}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_03218}; Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03218}; KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787, KW ECO:0000256|HAMAP-Rule:MF_03218}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_03218}; KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP- KW Rule:MF_03218}; Zinc {ECO:0000256|HAMAP-Rule:MF_03218}. FT DOMAIN 27..379 FT /note="tRNA-guanine(15) transglycosylase-like" FT /evidence="ECO:0000259|Pfam:PF01702" FT REGION 260..266 FT /note="RNA binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218" FT REGION 284..288 FT /note="RNA binding; important for wobble base 34 FT recognition" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218" FT ACT_SITE 105 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218" FT ACT_SITE 279 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218" FT BINDING 105..109 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218" FT BINDING 159 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218" FT BINDING 202 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218" FT BINDING 229 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218" FT BINDING 317 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218" FT BINDING 319 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218" FT BINDING 322 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218" FT BINDING 348 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218" SQ SEQUENCE 403 AA; 43990 MW; 1CCDDC17BF47A106 CRC64; MAGAATQASL ESAPRIMRLV AECSRSRARA GELWLPHGTV ATPVFMPVGT QATMKGITTE QLDALGCRIC LGNTYHLGLR PGPELIQKAN GLHGFMNWPH NLLTDSGGFQ MVSLVSLSEV TEEGVRFRSP YDGNETLLSP EKSVQIQNAL GSDIIMQLDD VVSSTVTGPR VEEAMYRSIR WLDRCIAAHQ RPDKQNLFAI IQGGLDADLR ATCLEEMTKR DVPGFAIGGL SGGESKSQFW RMVALSTSRL PKDKPRYLMG VGYATDLVVC VALGCDMFDC VFPTRTARFG SALVPTGNLQ LRKKVFEKDF GPIDPECTCP TCQKHSRAFL HALLHSDNTA ALHHLTVHNI AYQLQLMSAV RTSIVEKRFP GFVRDFMGAM YGDPTLCPTW ATDALASVGI TLG //