TGT_RAT
ID TGT_RAT Reviewed; 403 AA.
AC Q4QR99; Q9JMA0;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Queuine tRNA-ribosyltransferase catalytic subunit 1 {ECO:0000255|HAMAP-Rule:MF_03218};
DE EC=2.4.2.64 {ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:6986171};
DE AltName: Full=Guanine insertion enzyme {ECO:0000255|HAMAP-Rule:MF_03218};
DE AltName: Full=tRNA-guanine transglycosylase {ECO:0000255|HAMAP-Rule:MF_03218};
GN Name=Qtrt1 {ECO:0000255|HAMAP-Rule:MF_03218};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Hidaka T., Morishita T.;
RT "Rat tRNA-guanine transglycosylase (TGT).";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=6986171; DOI=10.1021/bi00543a023;
RA Shindo-Okada N., Okada N., Ohgi T., Goto T., Nishimura S.;
RT "Transfer ribonucleic acid guanine transglycosylase isolated from rat
RT liver.";
RL Biochemistry 19:395-400(1980).
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:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:6986171}.
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:0000255|HAMAP-
CC Rule:MF_03218, ECO:0000269|PubMed:6986171};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03218};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.29 uM for queuine {ECO:0000269|PubMed:6986171};
CC KM=2.1 uM for 7-aminomethyl-7-carbaguanine
CC {ECO:0000269|PubMed:6986171};
CC KM=0.83 uM for guanine {ECO:0000269|PubMed:6986171};
CC pH dependence:
CC Optimum pH is 7.3. {ECO:0000269|PubMed:6986171};
CC -!- SUBUNIT: Heterodimer of a catalytic subunit QTRT1 and an accessory
CC subunit QTRT2. {ECO:0000255|HAMAP-Rule:MF_03218}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03218}.
CC Mitochondrion outer membrane {ECO:0000255|HAMAP-Rule:MF_03218};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03218};
CC Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03218}. Note=Weakly
CC associates with mitochondria, possibly via QTRT2. {ECO:0000255|HAMAP-
CC Rule:MF_03218}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q4QR99-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q4QR99-2; Sequence=VSP_038056;
CC -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_03218}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA93552.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB034634; BAA93552.1; ALT_FRAME; mRNA.
DR EMBL; BC097321; AAH97321.1; -; mRNA.
DR RefSeq; NP_071586.2; NM_022250.2. [Q4QR99-1]
DR AlphaFoldDB; Q4QR99; -.
DR SMR; Q4QR99; -.
DR STRING; 10116.ENSRNOP00000010030; -.
DR ChEMBL; CHEMBL4395; -.
DR PaxDb; Q4QR99; -.
DR PRIDE; Q4QR99; -.
DR GeneID; 64016; -.
DR KEGG; rno:64016; -.
DR UCSC; RGD:620996; rat. [Q4QR99-1]
DR CTD; 81890; -.
DR RGD; 620996; Qtrt1.
DR eggNOG; KOG3908; Eukaryota.
DR HOGENOM; CLU_022060_0_1_1; -.
DR InParanoid; Q4QR99; -.
DR OrthoDB; 684306at2759; -.
DR PhylomeDB; Q4QR99; -.
DR TreeFam; TF300732; -.
DR PRO; PR:Q4QR99; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; Q4QR99; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:1990234; C:transferase complex; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0008479; F:queuine tRNA-ribosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0101030; P:tRNA-guanine transglycosylation; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Glycosyltransferase;
KW Membrane; Metal-binding; Mitochondrion; Mitochondrion outer membrane;
KW Phosphoprotein; Reference proteome; Transferase; tRNA processing; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9BXR0"
FT CHAIN 2..403
FT /note="Queuine tRNA-ribosyltransferase catalytic subunit 1"
FT /id="PRO_0000383946"
FT REGION 260..266
FT /note="RNA binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT REGION 284..288
FT /note="RNA binding; important for wobble base 34
FT recognition"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT ACT_SITE 105
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT ACT_SITE 279
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT BINDING 105..109
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT BINDING 317
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT BINDING 348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXR0"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXR0"
FT VAR_SEQ 354..403
FT /note="LQLLSAARSSILEQRFPDFVRNFMRTMYGDHSLCPAWAIEALASVGITLT
FT -> VTWMDMVWGREGLGSQGRVG (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_038056"
SQ SEQUENCE 403 AA; 44187 MW; A60C00474906A9F8 CRC64;
MAAVGSPGSL ESAPRIMRLV AECSRSRARA GELRLPHGTV ATPVFMPVGT QATMKGITAE
QLDSLGCRIC LGNTYHLGLR PGPELIQKAH GLHGFMNWPH NLLTDSGGFQ MVSLISLSEV
TEEGVRFRSP YDGEETLLSP ERSVEIQNAL GSDIIMQLDD VVSSTVTGPR VEEAMHRSVR
WLDRCIAAHK RQDKQNLFAI IQGGLNADLR TTCLKEMTKR DVPGFAIGGL SGGESKEQFW
KMVALSTSML PKDKPRYLMG VGYATDLVVC VALGCDMFDC VYPTRTARFG SALVPTGNLQ
LKKQQYAKDF SPINPECPCA TCQTHSRAFL HTLLHSDNTA ALHHLTVHNI AYQLQLLSAA
RSSILEQRFP DFVRNFMRTM YGDHSLCPAW AIEALASVGI TLT
