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Protein

Queuine tRNA-ribosyltransferase

Gene

tgt

Organism
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
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 annotation1 Publication

Catalytic activityi

Guanine(34) in tRNA + 7-aminomethyl-7-carbaguanine = 7-aminomethyl-7-carbaguanine(34) in tRNA + guanine.UniRule annotation1 Publication

Cofactori

Zn2+UniRule annotation10 PublicationsNote: Binds 1 zinc ion per subunit.UniRule annotation10 Publications

Kineticsi

kcat is 0.0022 sec(-1) with tRNA(Tyr) and guanine as substrates.1 Publication
  1. KM=0.2 µM for tRNA(Tyr)1 Publication
  2. KM=0.7 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 sitei102Proton acceptorUniRule annotation1 Publication1
    Binding sitei156SubstrateUniRule annotation1 Publication1
    Binding sitei203SubstrateUniRule annotation1 Publication1
    Binding sitei230Substrate; via amide nitrogenUniRule annotation1 Publication1
    Active sitei280NucleophileUniRule annotation1 Publication1
    Metal bindingi318ZincUniRule annotation10 Publications1
    Metal bindingi320ZincUniRule annotation10 Publications1
    Metal bindingi323ZincUniRule annotation10 Publications1
    Metal bindingi349Zinc; via pros nitrogenUniRule annotation10 Publications1

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

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

    Enzyme and pathway databases

    BRENDAi2.4.2.29 6765
    UniPathwayi
    UPA00392

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Queuine tRNA-ribosyltransferaseUniRule annotation (EC:2.4.2.29UniRule annotation)
    Alternative name(s):
    Guanine insertion enzymeUniRule annotation
    tRNA-guanine transglycosylaseUniRule annotation
    Gene namesi
    Name:tgtUniRule annotation
    Ordered Locus Names:ZMO0363
    OrganismiZymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
    Taxonomic identifieri264203 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeZymomonas
    Proteomesi
    • UP000001173 Componenti: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi103S → A: Strongly reduces activity. 1 Publication1
    Mutagenesisi156D → A: Abolishes catalytic activity. 1 Publication1
    Mutagenesisi280D → N: Abolishes catalytic activity. 1 Publication1

    Chemistry databases

    ChEMBLiCHEMBL2987
    DrugBankiDB04239 2-Amino-6-Aminomethyl-8-Phenylsulfanylmethyl-3h-Quinazolin-4-One
    DB01825 2-Amino-8-Methylquinazolin-4(3h)-One
    DB03780 2-Aminoquinazolin-4(3h)-One
    DB03304 7-Deaza-7-Aminomethyl-Guanine
    DB03074 7-Deaza-7-Cyano-Guanine
    DB02041 Isoluminol

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00001355632 – 386Queuine tRNA-ribosyltransferaseAdd BLAST385

    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 annotation2 Publications

    Chemistry databases

    BindingDBiP28720

    Structurei

    Secondary structure

    1386
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    ProteinModelPortaliP28720
    SMRiP28720
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP28720

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni102 – 106Substrate bindingUniRule annotation1 Publication5
    Regioni261 – 267RNA bindingUniRule annotation1 Publication7
    Regioni285 – 289RNA binding; important for wobble base 34 recognitionUniRule annotation1 Publication5

    Sequence similaritiesi

    Belongs to the queuine tRNA-ribosyltransferase family.UniRule annotation

    Phylogenomic databases

    HOGENOMiHOG000223473
    KOiK00773
    OMAiGIDLFDC

    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.

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

    P28720-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MVEATAQETD RPRFSFSIAA REGKARTGTI EMKRGVIRTP AFMPVGTAAT
    60 70 80 90 100
    VKALKPETVR ATGADIILGN TYHLMLRPGA ERIAKLGGLH SFMGWDRPIL
    110 120 130 140 150
    TDSGGYQVMS LSSLTKQSEE GVTFKSHLDG SRHMLSPERS IEIQHLLGSD
    160 170 180 190 200
    IVMAFDECTP YPATPSRAAS SMERSMRWAK RSRDAFDSRK EQAENAALFG
    210 220 230 240 250
    IQQGSVFENL RQQSADALAE IGFDGYAVGG LAVGEGQDEM FRVLDFSVPM
    260 270 280 290 300
    LPDDKPHYLM GVGKPDDIVG AVERGIDMFD CVLPTRSGRN GQAFTWDGPI
    310 320 330 340 350
    NIRNARFSED LTPLDSECHC AVCQKWSRAY IHHLIRAGEI LGAMLMTEHN
    360 370 380
    IAFYQQLMQK IRDSISEGRF SQFAQDFRAR YFARNS
    Length:386
    Mass (Da):42,843
    Last modified:January 23, 2007 - v4
    Checksum:i26754E08600BD941
    GO

    Sequence cautioni

    The sequence AAA27704 differs from that shown. Reason: Erroneous initiation.Curated
    The sequence AAA27705 differs from that shown. Reason: Erroneous initiation.Curated
    The sequence AAG29862 differs from that shown. Reason: Erroneous initiation.Curated
    The sequence Z11910 differs from that shown. Reason: Frameshift at several positions.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti312T → K (PubMed:7665516).Curated1
    Sequence conflicti312T → K (Ref. 2) Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L33777 Genomic DNA Translation: AAA27704.1 Different initiation.
    L33777 Genomic DNA Translation: AAA27705.1 Different initiation.
    AF313764 Genomic DNA Translation: AAG29862.1 Different initiation.
    AE008692 Genomic DNA Translation: AAV88987.2
    Z11910 Genomic DNA No translation available.
    PIRiT46898

    Genome annotation databases

    EnsemblBacteriaiAAV88987; AAV88987; ZMO0363
    KEGGizmo:ZMO0363

    Similar proteinsi

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L33777 Genomic DNA Translation: AAA27704.1 Different initiation.
    L33777 Genomic DNA Translation: AAA27705.1 Different initiation.
    AF313764 Genomic DNA Translation: AAG29862.1 Different initiation.
    AE008692 Genomic DNA Translation: AAV88987.2
    Z11910 Genomic DNA No translation available.
    PIRiT46898

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1EFZX-ray2.00A1-386[»]
    1ENUX-ray1.95A1-386[»]
    1F3EX-ray1.85A1-386[»]
    1K4GX-ray1.70A1-386[»]
    1K4HX-ray1.80A1-386[»]
    1N2VX-ray2.10A1-386[»]
    1OZMX-ray1.95A2-386[»]
    1OZQX-ray1.90A2-386[»]
    1P0BX-ray1.70A2-386[»]
    1P0DX-ray1.90A2-386[»]
    1P0EX-ray2.40A2-386[»]
    1PUDX-ray1.85A1-386[»]
    1PXGX-ray1.70A2-383[»]
    1Q2RX-ray2.90A/B/C/D1-386[»]
    1Q2SX-ray3.20A/B/C/D1-386[»]
    1Q4WX-ray1.93A1-386[»]
    1Q63X-ray1.85A1-386[»]
    1Q65X-ray2.10A1-386[»]
    1Q66X-ray1.75A1-386[»]
    1R5YX-ray1.20A1-386[»]
    1S38X-ray1.81A1-386[»]
    1S39X-ray1.95A1-386[»]
    1WKDX-ray2.60A1-386[»]
    1WKEX-ray2.20A1-386[»]
    1WKFX-ray2.20A1-386[»]
    1Y5VX-ray1.58A2-386[»]
    1Y5WX-ray1.58A2-386[»]
    1Y5XX-ray2.10A/D2-386[»]
    2BBFX-ray1.70A1-386[»]
    2NQZX-ray1.46A2-386[»]
    2NSOX-ray1.60A1-386[»]
    2OKOX-ray1.50A2-386[»]
    2POTX-ray1.80A1-386[»]
    2PWUX-ray1.77A1-386[»]
    2PWVX-ray1.70A1-386[»]
    2QIIX-ray1.70A1-386[»]
    2QZRX-ray1.95A2-386[»]
    2Z1VX-ray1.55A1-386[»]
    2Z1WX-ray1.63A1-386[»]
    2Z1XX-ray1.63A1-386[»]
    2Z7KX-ray1.28A1-386[»]
    3BL3X-ray2.25A1-386[»]
    3BLDX-ray1.19A1-386[»]
    3BLLX-ray1.26A1-386[»]
    3BLOX-ray1.60A1-386[»]
    3C2YX-ray1.78A1-386[»]
    3EOSX-ray1.78A1-386[»]
    3EOUX-ray1.93A1-386[»]
    3GC4X-ray1.80A1-386[»]
    3GC5X-ray1.40A1-386[»]
    3GE7X-ray1.50A1-386[»]
    3HFYX-ray2.00A1-386[»]
    3RR4X-ray1.68A1-386[»]
    3S1GX-ray1.82A1-386[»]
    3SM0X-ray1.57A1-386[»]
    3TLLX-ray1.37A1-386[»]
    3UNTX-ray1.80A1-386[»]
    3UVIX-ray1.55A1-386[»]
    4DXXX-ray1.66A1-386[»]
    4DY1X-ray2.04A1-386[»]
    4E2VX-ray1.18A1-386[»]
    4FPSX-ray1.45A1-386[»]
    4FR1X-ray1.74A1-386[»]
    4FR6X-ray1.59A1-386[»]
    4FSAX-ray1.62A1-386[»]
    4GCXX-ray1.42A1-386[»]
    4GD0X-ray1.29A1-386[»]
    4GG9X-ray1.48A1-386[»]
    4GH1X-ray1.45A1-386[»]
    4GH3X-ray2.06A1-386[»]
    4GHRX-ray2.00A1-386[»]
    4GI4X-ray1.97A1-386[»]
    4GIYX-ray1.75A1-386[»]
    4GKTX-ray1.53A1-386[»]
    4H6EX-ray1.42A1-386[»]
    4H7ZX-ray1.68A1-386[»]
    4HQVX-ray1.66A2-386[»]
    4HSHX-ray1.56A2-386[»]
    4HTBX-ray1.90A1-386[»]
    4HVXX-ray1.82A1-386[»]
    4IPPX-ray1.33A1-386[»]
    4JBRX-ray2.92A1-386[»]
    4KWOX-ray1.32A1-386[»]
    4L56X-ray1.70A1-386[»]
    4LBUX-ray1.17A1-386[»]
    4LEQX-ray1.40A1-386[»]
    4PUJX-ray1.42A1-386[»]
    4PUKX-ray1.49A1-386[»]
    4PULX-ray1.65A1-386[»]
    4PUMX-ray1.93A1-386[»]
    4PUNX-ray1.25A1-386[»]
    4Q4MX-ray1.62A1-386[»]
    4Q4OX-ray1.35A1-386[»]
    4Q4PX-ray1.54A1-386[»]
    4Q4QX-ray1.41A1-386[»]
    4Q4RX-ray1.45A1-386[»]
    4Q4SX-ray1.25A1-386[»]
    4Q8MX-ray1.24A1-386[»]
    4Q8NX-ray1.45A1-386[»]
    4Q8OX-ray1.89A1-386[»]
    4Q8PX-ray1.45A1-386[»]
    4Q8QX-ray1.72A1-386[»]
    4Q8TX-ray1.40A1-386[»]
    4Q8UX-ray1.31A1-386[»]
    4Q8VX-ray1.40A1-386[»]
    4Q8WX-ray1.14A1-386[»]
    5EGRX-ray1.55A1-386[»]
    5I00X-ray1.49A1-385[»]
    5I02X-ray1.25A1-385[»]
    5I03X-ray1.73A1-386[»]
    5I06X-ray1.36A1-386[»]
    5I07X-ray1.89A/B1-386[»]
    5I09X-ray1.44A1-386[»]
    5J9MX-ray1.33A1-386[»]
    5J9NX-ray1.64A1-386[»]
    5J9OX-ray1.41A1-386[»]
    5JGMX-ray1.38A1-386[»]
    5JGOX-ray1.37A1-386[»]
    5JSVX-ray1.17A1-386[»]
    5JSWX-ray1.22A1-386[»]
    5JT5X-ray1.21A1-386[»]
    5JT6X-ray1.54A1-386[»]
    5JT7X-ray1.70A1-386[»]
    5JXQX-ray1.20A1-386[»]
    5LPOX-ray1.42A1-386[»]
    5LPPX-ray1.99A1-386[»]
    5LPQX-ray2.52A/B1-386[»]
    5LPSX-ray1.27A1-386[»]
    5LPTX-ray2.36A/B1-386[»]
    5N6FX-ray1.12A10-384[»]
    5SW3X-ray1.38A10-384[»]
    5UTIX-ray1.36A10-384[»]
    5UTJX-ray1.55A10-384[»]
    5V3CX-ray1.42A10-384[»]
    ProteinModelPortaliP28720
    SMRiP28720
    ModBaseiSearch...
    MobiDBiSearch...

    Chemistry databases

    BindingDBiP28720
    ChEMBLiCHEMBL2987
    DrugBankiDB04239 2-Amino-6-Aminomethyl-8-Phenylsulfanylmethyl-3h-Quinazolin-4-One
    DB01825 2-Amino-8-Methylquinazolin-4(3h)-One
    DB03780 2-Aminoquinazolin-4(3h)-One
    DB03304 7-Deaza-7-Aminomethyl-Guanine
    DB03074 7-Deaza-7-Cyano-Guanine
    DB02041 Isoluminol

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAV88987; AAV88987; ZMO0363
    KEGGizmo:ZMO0363

    Phylogenomic databases

    HOGENOMiHOG000223473
    KOiK00773
    OMAiGIDLFDC

    Enzyme and pathway databases

    UniPathwayi
    UPA00392

    BRENDAi2.4.2.29 6765

    Miscellaneous databases

    EvolutionaryTraceiP28720
    PROiPR:P28720

    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
    ProtoNetiSearch...

    Entry informationi

    Entry nameiTGT_ZYMMO
    AccessioniPrimary (citable) accession number: P28720
    Secondary accession number(s): Q5NQL7, Q60247, Q9F5L7
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: January 23, 2007
    Last modified: November 7, 2018
    This is version 160 of the entry and version 4 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
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