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-NOV-2016, entry version 53. DE RecName: Full=Queuine tRNA-ribosyltransferase catalytic subunit 1 {ECO:0000256|HAMAP-Rule:MF_03218}; DE EC=2.4.2.29 {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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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 RT 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 CC with queuine (Q) at position 34 (anticodon wobble position) in CC tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), CC resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis- CC dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). CC Catalysis occurs through a double-displacement mechanism. The CC nucleophile active site attacks the C1' of nucleotide 34 to detach CC the guanine base from the RNA, forming a covalent enzyme-RNA CC intermediate. The proton acceptor active site deprotonates the CC incoming queuine, allowing a nucleophilic attack on the C1' of the CC ribose to form the product. {ECO:0000256|HAMAP-Rule:MF_03218}. 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|RuleBase:RU003777}. CC -!- CATALYTIC ACTIVITY: Guanine(34) in tRNA + 7-aminomethyl-7- CC carbaguanine = 7-aminomethyl-7-carbaguanine(34) in tRNA + guanine. CC {ECO:0000256|RuleBase:RU003777}. CC -!- CATALYTIC ACTIVITY: Guanine(34) in tRNA + queuine = queuosine(34) CC in tRNA + guanine. {ECO:0000256|HAMAP-Rule:MF_03218}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03218}; CC -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis. CC {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. CC {ECO:0000256|HAMAP-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 UniGene; Hs.631638; -. DR STRING; 9606.ENSP00000250237; -. DR PaxDb; B2RAR3; -. DR PeptideAtlas; B2RAR3; -. DR PRIDE; B2RAR3; -. DR eggNOG; KOG3908; Eukaryota. DR eggNOG; COG0343; LUCA. DR HOVERGEN; HBG101131; -. DR UniPathway; UPA00392; -. DR GO; GO:0008479; F:queuine tRNA-ribosyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006400; P:tRNA modification; IEA:InterPro. DR Gene3D; 3.20.20.105; -; 1. DR HAMAP; MF_00168; Q_tRNA_Tgt; 1. DR InterPro; IPR004803; Queuine_tRNA-ribosylTrfase. 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|HAMAP-Rule:MF_03218, KW ECO:0000256|RuleBase:RU003777}; KW 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|HAMAP-Rule:MF_03218}; KW Queuosine biosynthesis {ECO:0000256|HAMAP-Rule:MF_03218, KW ECO:0000256|RuleBase:RU003777}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_03218, KW ECO:0000256|RuleBase:RU003777, ECO:0000313|EMBL:BAG36960.1}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_03218, KW ECO:0000256|RuleBase:RU003777}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_03218, ECO:0000256|RuleBase:RU003777}. FT REGION 105 109 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_03218}. FT REGION 260 266 RNA binding. {ECO:0000256|HAMAP-Rule: FT MF_03218}. FT REGION 284 288 RNA binding; important for wobble base 34 FT recognition. {ECO:0000256|HAMAP-Rule: FT MF_03218}. FT ACT_SITE 105 105 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_03218}. FT ACT_SITE 279 279 Nucleophile. {ECO:0000256|HAMAP-Rule: FT MF_03218}. FT METAL 317 317 Zinc. {ECO:0000256|HAMAP-Rule:MF_03218}. FT METAL 319 319 Zinc. {ECO:0000256|HAMAP-Rule:MF_03218}. FT METAL 322 322 Zinc. {ECO:0000256|HAMAP-Rule:MF_03218}. FT METAL 348 348 Zinc; via pros nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_03218}. FT BINDING 159 159 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_03218}. FT BINDING 202 202 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_03218}. FT BINDING 229 229 Substrate; via amide nitrogen. FT {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 //