Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Queuine tRNA-ribosyltransferase

Gene

tgt

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GUN anticodons (tRNA-Asp, -Asn, -His and -Tyr). 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 PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).UniRule annotation2 Publications

Catalytic activityi

Guanine(34) in tRNA + 7-aminomethyl-7-carbaguanine = 7-aminomethyl-7-carbaguanine(34) in tRNA + guanine.UniRule annotation2 Publications

Cofactori

Zn2+UniRule annotation1 PublicationNote: Binds 1 zinc ion per subunit.UniRule annotation1 Publication

Kineticsi

kcat is 0.00121 sec(-1) with tRNA(Tyr) and guanine as substrates.1 Publication
  1. KM=0.12 µM for tRNA(Tyr)1 Publication
  2. KM=0.1 µM for guanine1 Publication

    Pathwayi: tRNA-queuosine biosynthesis

    This protein is involved in the pathway tRNA-queuosine biosynthesis, which is part of tRNA modification.UniRule annotation1 Publication
    View all proteins of this organism that are known to be involved in the pathway tRNA-queuosine biosynthesis and in tRNA modification.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei89Proton acceptorUniRule annotation1 Publication1
    Binding sitei143SubstrateUniRule annotation1
    Binding sitei187SubstrateUniRule annotation1
    Binding sitei214Substrate; via amide nitrogenUniRule annotation1
    Active sitei264NucleophileUniRule annotation1 Publication1
    Metal bindingi302ZincUniRule annotation1 Publication1
    Metal bindingi304ZincUniRule annotation1 Publication1
    Metal bindingi307ZincUniRule annotation1 Publication1
    Metal bindingi333Zinc; via pros nitrogenUniRule annotation1

    GO - Molecular functioni

    • queuine tRNA-ribosyltransferase activity Source: EcoCyc
    • zinc ion binding Source: EcoCyc

    GO - Biological processi

    • queuosine biosynthetic process Source: EcoCyc
    • tRNA-guanine transglycosylation Source: InterPro
    • tRNA wobble guanine modification Source: EcoCyc

    Keywordsi

    Molecular functionGlycosyltransferase, Transferase
    Biological processQueuosine biosynthesis, tRNA processing
    LigandMetal-binding, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10996-MONOMER
    MetaCyc:EG10996-MONOMER
    BRENDAi2.4.2.29 2026
    SABIO-RKiP0A847
    UniPathwayiUPA00392

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Queuine tRNA-ribosyltransferaseUniRule annotation (EC:2.4.2.29UniRule annotation2 Publications)
    Alternative name(s):
    Guanine insertion enzymeUniRule annotation
    tRNA-guanine transglycosylaseUniRule annotation
    Gene namesi
    Name:tgtUniRule annotation
    Ordered Locus Names:b0406, JW0396
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10996 tgt

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi28C → A: Slight loss of activity. 1 Publication1
    Mutagenesisi89D → E: Reduces catalytic activity by 51%. 1 Publication1
    Mutagenesisi90S → A: Loss of activity. 1 Publication1
    Mutagenesisi90S → C: Loss of activity. 1 Publication1
    Mutagenesisi90S → F: Loss of activity. 1 Publication1
    Mutagenesisi145C → A: No loss of activity. 1 Publication1
    Mutagenesisi232C → A: Slight loss of activity. 1 Publication1
    Mutagenesisi264D → A, N, Q, K or H: Loss of catalytic activity. 1 Publication1
    Mutagenesisi264D → E: Reduces catalytic activity by 88%. 1 Publication1
    Mutagenesisi265C → A: Significant loss of activity. 1 Publication1
    Mutagenesisi302C → A: Loss of activity. 1 Publication1
    Mutagenesisi304C → A: Loss of activity. 1 Publication1
    Mutagenesisi307C → A: Loss of activity. 1 Publication1
    Mutagenesisi316H → A: Slight loss of activity. 1 Publication1
    Mutagenesisi317H → A: Loss of activity. 1 Publication1
    Mutagenesisi321C → A: No loss of activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001354711 – 375Queuine tRNA-ribosyltransferaseAdd BLAST375

    Proteomic databases

    EPDiP0A847
    PaxDbiP0A847
    PRIDEiP0A847

    Interactioni

    Subunit structurei

    Homodimer. Within each dimer, one monomer is responsible for RNA recognition and catalysis, while the other monomer binds to the replacement base PreQ1.UniRule annotation

    Protein-protein interaction databases

    BioGridi4263531, 21 interactors
    DIPiDIP-36020N
    IntActiP0A847, 39 interactors
    STRINGi316385.ECDH10B_0362

    Structurei

    3D structure databases

    ProteinModelPortaliP0A847
    SMRiP0A847
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni89 – 93Substrate bindingUniRule annotation5
    Regioni245 – 251RNA bindingUniRule annotation7
    Regioni269 – 273RNA binding; important for wobble base 34 recognitionUniRule annotation5

    Sequence similaritiesi

    Belongs to the queuine tRNA-ribosyltransferase family.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4105C6U Bacteria
    COG0343 LUCA
    HOGENOMiHOG000223473
    InParanoidiP0A847
    KOiK00773
    OMAiTYHLFLR
    PhylomeDBiP0A847

    Family and domain databases

    Gene3Di3.20.20.105, 1 hit
    HAMAPiMF_00168 Q_tRNA_Tgt, 1 hit
    InterProiView protein in InterPro
    IPR004803 TGT
    IPR036511 TGT-like_sf
    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

    Sequencei

    Sequence statusi: Complete.

    P0A847-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKFELDTTDG RARRGRLVFD RGVVETPCFM PVGTYGTVKG MTPEEVEATG
    60 70 80 90 100
    AQIILGNTFH LWLRPGQEIM KLHGDLHDFM QWKGPILTDS GGFQVFSLGD
    110 120 130 140 150
    IRKITEQGVH FRNPINGDPI FLDPEKSMEI QYDLGSDIVM IFDECTPYPA
    160 170 180 190 200
    DWDYAKRSME MSLRWAKRSR ERFDSLGNKN ALFGIIQGSV YEDLRDISVK
    210 220 230 240 250
    GLVDIGFDGY AVGGLAVGEP KADMHRILEH VCPQIPADKP RYLMGVGKPE
    260 270 280 290 300
    DLVEGVRRGI DMFDCVMPTR NARNGHLFVT DGVVKIRNAK YKSDTGPLDP
    310 320 330 340 350
    ECDCYTCRNY SRAYLHHLDR CNEILGARLN TIHNLRYYQR LMAGLRKAIE
    360 370
    EGKLESFVTD FYQRQGREVP PLNVD
    Length:375
    Mass (Da):42,594
    Last modified:June 7, 2005 - v1
    Checksum:i40271CA08D8A8820
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti54 – 55IL → MV (PubMed:1706703).Curated2
    Sequence conflicti54 – 55IL → MV (PubMed:8323579).Curated2

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M63939 Genomic DNA Translation: AAA24667.1
    U00096 Genomic DNA Translation: AAC73509.1
    AP009048 Genomic DNA Translation: BAE76186.1
    U82664 Genomic DNA Translation: AAB40162.1
    X56175 Genomic DNA Translation: CAA39631.1 Sequence problems.
    X56175 Genomic DNA Translation: CAA39632.1 Sequence problems.
    S68715 Genomic DNA Translation: AAC60467.2
    PIRiC38530
    RefSeqiNP_414940.1, NC_000913.3
    WP_000667319.1, NZ_LN832404.1

    Genome annotation databases

    EnsemblBacteriaiAAC73509; AAC73509; b0406
    BAE76186; BAE76186; BAE76186
    GeneIDi949130
    KEGGiecj:JW0396
    eco:b0406
    PATRICifig|1411691.4.peg.1871

    Similar proteinsi

    Entry informationi

    Entry nameiTGT_ECOLI
    AccessioniPrimary (citable) accession number: P0A847
    Secondary accession number(s): P19675
    , P19676, P78226, Q2MC20, Q47627
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: June 7, 2005
    Last modified: March 28, 2018
    This is version 107 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health