ID B2RAR3_HUMAN Unreviewed; 403 AA. AC B2RAR3; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 02-JUN-2021, entry version 70. 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 -!- 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|RuleBase:RU003777}. 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; CC Evidence={ECO:0000256|RuleBase:RU003777}; 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:10345, ChEBI:CHEBI:16235, ChEBI:CHEBI:74269, ChEBI:CHEBI:77674, CC ChEBI:CHEBI:82831; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|RuleBase:RU003777}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU003777}; 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, 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; AK314308; BAG36960.1; -; mRNA. DR PeptideAtlas; B2RAR3; -. DR PRIDE; B2RAR3; -. DR OMA; GIDLFDC; -. DR ChiTaRS; QTRT1; human. 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:queuine tRNA-ribosyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0101030; P:tRNA-guanine transglycosylation; IEA:UniProtKB-UniRule. 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 2: Evidence at transcript level; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03218}; KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP- KW Rule:MF_03218}; Membrane {ECO:0000256|HAMAP-Rule:MF_03218}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03218}; KW 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}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_03218, ECO:0000256|RuleBase:RU003777}. FT DOMAIN 27..380 FT /note="TGT" FT /evidence="ECO:0000259|Pfam:PF01702" FT REGION 105..109 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218" 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 METAL 317 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218" FT METAL 319 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218" FT METAL 322 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218" FT METAL 348 FT /note="Zinc; via pros nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218" FT BINDING 159 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218" FT BINDING 202 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218" FT BINDING 229 FT /note="Substrate; via amide nitrogen" 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 //