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Protein

Queuine tRNA-ribosyltransferase catalytic subunit 1

Gene

QTRT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GUN anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine) (PubMed:11255023, PubMed:20354154). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming queuine, allowing a nucleophilic attack on the C1' of the ribose to form the product (By similarity).UniRule annotationBy similarity2 Publications

Catalytic activityi

Guanine(34) in tRNA + queuine = queuosine(34) in tRNA + guanine.UniRule annotation1 Publication

Cofactori

Zn2+UniRule annotation

Kineticsi

kcat is 0.0056 sec(-1) with tRNA(Tyr) as substrate and 0.00586 sec(-1) with guanine as substrate.1 Publication
  1. KM=0.34 µM for tRNA(Tyr)1 Publication
  2. KM=0.41 µM for guanine1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei105Proton acceptorUniRule annotation1
    Binding sitei159SubstrateUniRule annotation1
    Binding sitei202SubstrateUniRule annotation1
    Binding sitei229Substrate; via amide nitrogenUniRule annotation1
    Active sitei279NucleophileUniRule annotation1
    Metal bindingi317ZincUniRule annotation1
    Metal bindingi319ZincUniRule annotation1
    Metal bindingi322ZincUniRule annotation1
    Metal bindingi348Zinc; via pros nitrogenUniRule annotation1

    GO - Molecular functioni

    • metal ion binding Source: UniProtKB-KW
    • protein heterodimerization activity Source: UniProtKB
    • protein homodimerization activity Source: UniProtKB
    • queuine tRNA-ribosyltransferase activity Source: UniProtKB

    GO - Biological processi

    • tRNA-guanine transglycosylation Source: UniProtKB
    • tRNA modification Source: UniProtKB

    Keywordsi

    Molecular functionGlycosyltransferase, Transferase
    Biological processtRNA processing
    LigandMetal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi2.4.2.29. 2681.
    ReactomeiR-HSA-6782315. tRNA modification in the nucleus and cytosol.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Queuine tRNA-ribosyltransferase catalytic subunit 1UniRule annotation (EC:2.4.2.29UniRule annotation1 Publication)
    Alternative name(s):
    Guanine insertion enzymeUniRule annotation
    tRNA-guanine transglycosylaseUniRule annotation
    Gene namesi
    Name:QTRT1UniRule annotation
    Synonyms:TGT, TGUT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:23797. QTRT1.

    Subcellular locationi

    • Cytoplasm UniRule annotation
    • Mitochondrion outer membrane UniRule annotation; Peripheral membrane protein UniRule annotation; Cytoplasmic side UniRule annotation

    • Note: Weakly associates with mitochondria, possibly via QTRT2.UniRule annotation

    GO - Cellular componenti

    • mitochondrial outer membrane Source: Reactome
    • nucleus Source: Ensembl
    • protein complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi279D → N: Loss of transglycosylase activity. 1 Publication1

    Organism-specific databases

    DisGeNETi81890.
    OpenTargetsiENSG00000213339.
    PharmGKBiPA134963074.

    Chemistry databases

    ChEMBLiCHEMBL6004.

    Polymorphism and mutation databases

    BioMutaiQTRT1.
    DMDMi239938842.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemovedCombined sources
    ChainiPRO_00001355652 – 403Queuine tRNA-ribosyltransferase catalytic subunit 1Add BLAST402

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei2N-acetylalanineCombined sources1
    Modified residuei139PhosphoserineCombined sources1

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    EPDiQ9BXR0.
    MaxQBiQ9BXR0.
    PaxDbiQ9BXR0.
    PeptideAtlasiQ9BXR0.
    PRIDEiQ9BXR0.

    PTM databases

    iPTMnetiQ9BXR0.
    PhosphoSitePlusiQ9BXR0.

    Expressioni

    Gene expression databases

    BgeeiENSG00000213339.
    CleanExiHS_QTRT1.
    ExpressionAtlasiQ9BXR0. baseline and differential.
    GenevisibleiQ9BXR0. HS.

    Organism-specific databases

    HPAiHPA042695.
    HPA048651.
    HPA049440.

    Interactioni

    Subunit structurei

    Heterodimer of a catalytic subunit QTRT1 and an accessory subunit QTRT2.UniRule annotation1 Publication

    GO - Molecular functioni

    • protein heterodimerization activity Source: UniProtKB
    • protein homodimerization activity Source: UniProtKB

    Protein-protein interaction databases

    BioGridi123623. 18 interactors.
    IntActiQ9BXR0. 7 interactors.
    MINTiMINT-4656737.
    STRINGi9606.ENSP00000250237.

    Chemistry databases

    BindingDBiQ9BXR0.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BXR0.
    SMRiQ9BXR0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni105 – 109Substrate bindingUniRule annotation5
    Regioni260 – 266RNA bindingUniRule annotation7
    Regioni284 – 288RNA binding; important for wobble base 34 recognitionUniRule annotation5

    Sequence similaritiesi

    Belongs to the queuine tRNA-ribosyltransferase family.UniRule annotation

    Phylogenomic databases

    eggNOGiKOG3908. Eukaryota.
    COG0343. LUCA.
    GeneTreeiENSGT00530000063679.
    HOGENOMiHOG000223473.
    HOVERGENiHBG101131.
    InParanoidiQ9BXR0.
    KOiK00773.
    OMAiTYHLFLR.
    OrthoDBiEOG091G09KJ.
    PhylomeDBiQ9BXR0.
    TreeFamiTF300732.

    Family and domain databases

    Gene3Di3.20.20.105. 1 hit.
    HAMAPiMF_00168. Q_tRNA_Tgt. 1 hit.
    InterProiView protein in InterPro
    IPR004803. TGT.
    IPR002616. tRNA_ribo_trans-like.
    PfamiView protein in Pfam
    PF01702. TGT. 1 hit.
    SUPFAMiSSF51713. SSF51713. 1 hit.
    TIGRFAMsiTIGR00430. Q_tRNA_tgt. 1 hit.
    TIGR00449. tgt_general. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q9BXR0-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MAGAATQASL ESAPRIMRLV AECSRSRARA GELWLPHGTV ATPVFMPVGT
    60 70 80 90 100
    QATMKGITTE QLDALGCRIC LGNTYHLGLR PGPELIQKAN GLHGFMNWPH
    110 120 130 140 150
    NLLTDSGGFQ MVSLVSLSEV TEEGVRFRSP YDGNETLLSP EKSVQIQNAL
    160 170 180 190 200
    GSDIIMQLDD VVSSTVTGPR VEEAMYRSIR WLDRCIAAHQ RPDKQNLFAI
    210 220 230 240 250
    IQGGLDADLR ATCLEEMTKR DVPGFAIGGL SGGESKSQFW RMVALSTSRL
    260 270 280 290 300
    PKDKPRYLMG VGYATDLVVC VALGCDMFDC VFPTRTARFG SALVPTGNLQ
    310 320 330 340 350
    LRKKVFEKDF GPIDPECTCP TCQKHSRAFL HALLHSDNTA ALHHLTVHNI
    360 370 380 390 400
    AYQLQLMSAV RTSIVEKRFP DFVRDFMGAM YGDPTLCPTW ATDALASVGI

    TLG
    Length:403
    Mass (Da):44,048
    Last modified:June 16, 2009 - v3
    Checksum:i1E30F3C7BF47A106
    GO
    Isoform 2 (identifier: Q9BXR0-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         178-225: SIRWLDRCIA...EMTKRDVPGF → PLGLVTGALL...AGRRSPGHLP
         226-403: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:225
    Mass (Da):24,015
    Checksum:iC62B238F305E24A9
    GO

    Sequence cautioni

    The sequence AAH15350 differs from that shown. Reason: Erroneous initiation.Curated

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_056470178 – 225SIRWL…DVPGF → PLGLVTGALLQVNPLAGPVH CSPSAAGQAEPLRHYPGWAG RRSPGHLP in isoform 2. 1 PublicationAdd BLAST48
    Alternative sequenceiVSP_056471226 – 403Missing in isoform 2. 1 PublicationAdd BLAST178

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF302783 mRNA. Translation: AAG60033.1.
    AF302784 mRNA. Translation: AAG60034.1.
    AK294166 mRNA. Translation: BAG57488.1.
    AC011475 Genomic DNA. No translation available.
    BC015350 mRNA. Translation: AAH15350.1. Different initiation.
    CCDSiCCDS12248.1. [Q9BXR0-1]
    RefSeqiNP_112486.1. NM_031209.2. [Q9BXR0-1]
    UniGeneiHs.631638.

    Genome annotation databases

    EnsembliENST00000250237; ENSP00000250237; ENSG00000213339. [Q9BXR0-1]
    ENST00000421333; ENSP00000389126; ENSG00000213339. [Q9BXR0-2]
    GeneIDi81890.
    KEGGihsa:81890.
    UCSCiuc002mpr.4. human. [Q9BXR0-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Similar proteinsi

    Entry informationi

    Entry nameiTGT_HUMAN
    AccessioniPrimary (citable) accession number: Q9BXR0
    Secondary accession number(s): B4DFM7, Q96BQ4, Q9BXQ9
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 2, 2002
    Last sequence update: June 16, 2009
    Last modified: August 30, 2017
    This is version 144 of the entry and version 3 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families