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Database: UniProt
Entry: A0A1F6DWT3_9BACT
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ID   A0A1F6DWT3_9BACT        Unreviewed;       378 AA.
AC   A0A1F6DWT3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   08-NOV-2023, entry version 23.
DE   RecName: Full=Queuine tRNA-ribosyltransferase {ECO:0000256|HAMAP-Rule:MF_00168};
DE            EC=2.4.2.29 {ECO:0000256|HAMAP-Rule:MF_00168};
DE   AltName: Full=Guanine insertion enzyme {ECO:0000256|HAMAP-Rule:MF_00168};
DE   AltName: Full=tRNA-guanine transglycosylase {ECO:0000256|HAMAP-Rule:MF_00168};
GN   Name=tgt {ECO:0000256|HAMAP-Rule:MF_00168};
GN   ORFNames=A3D71_00600 {ECO:0000313|EMBL:OGG65856.1};
OS   Candidatus Kaiserbacteria bacterium RIFCSPHIGHO2_02_FULL_55_20.
OC   Bacteria; Candidatus Kaiserbacteria.
OX   NCBI_TaxID=1798497 {ECO:0000313|EMBL:OGG65856.1, ECO:0000313|Proteomes:UP000177652};
RN   [1] {ECO:0000313|EMBL:OGG65856.1, ECO:0000313|Proteomes:UP000177652}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
CC   -!- FUNCTION: Catalyzes the base-exchange of a guanine (G) residue with the
CC       queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34
CC       (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp,
CC       -Asn, -His and -Tyr). Catalysis occurs through a double-displacement
CC       mechanism. The nucleophile active site attacks the C1' of nucleotide 34
CC       to detach the guanine base from the RNA, forming a covalent enzyme-RNA
CC       intermediate. The proton acceptor active site deprotonates the incoming
CC       PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form
CC       the product. After dissociation, two additional enzymatic reactions on
CC       the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified
CC       nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-
CC       yl)amino)methyl)-7-deazaguanosine). {ECO:0000256|HAMAP-Rule:MF_00168}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7-aminomethyl-7-carbaguanine + guanosine(34) in tRNA = 7-
CC         aminomethyl-7-carbaguanosine(34) in tRNA + guanine;
CC         Xref=Rhea:RHEA:24104, Rhea:RHEA-COMP:10341, Rhea:RHEA-COMP:10342,
CC         ChEBI:CHEBI:16235, ChEBI:CHEBI:58703, ChEBI:CHEBI:74269,
CC         ChEBI:CHEBI:82833; EC=2.4.2.29; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00168};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00168};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00168};
CC   -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00168}.
CC   -!- SUBUNIT: Homodimer. Within each dimer, one monomer is responsible for
CC       RNA recognition and catalysis, while the other monomer binds to the
CC       replacement base PreQ1. {ECO:0000256|HAMAP-Rule:MF_00168}.
CC   -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00168}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00168}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OGG65856.1}.
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DR   EMBL; MFLK01000029; OGG65856.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F6DWT3; -.
DR   STRING; 1798497.A3D71_00600; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000177652; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008479; F:tRNA-guanosine(34) queuine transglycosylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0101030; P:tRNA-guanine transglycosylation; IEA:InterPro.
DR   Gene3D; 3.20.20.105; Queuine tRNA-ribosyltransferase-like; 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   NCBIfam; TIGR00430; Q_tRNA_tgt; 1.
DR   NCBIfam; TIGR00449; tgt_general; 1.
DR   PANTHER; PTHR46499; QUEUINE TRNA-RIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR46499:SF1; QUEUINE TRNA-RIBOSYLTRANSFERASE; 1.
DR   Pfam; PF01702; TGT; 1.
DR   SUPFAM; SSF51713; tRNA-guanine transglycosylase; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW   Rule:MF_00168}; Metal-binding {ECO:0000256|HAMAP-Rule:MF_00168};
KW   Queuosine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00168};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00168};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_00168}; Zinc {ECO:0000256|HAMAP-Rule:MF_00168}.
FT   DOMAIN          14..377
FT                   /note="tRNA-guanine(15) transglycosylase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01702"
FT   REGION          269..275
FT                   /note="RNA binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   ACT_SITE        92
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   ACT_SITE        288
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   BINDING         92..96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   BINDING         171
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   BINDING         212
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   BINDING         239
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   BINDING         326
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   BINDING         328
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   BINDING         331
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   BINDING         357
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
SQ   SEQUENCE   378 AA;  42627 MW;  1A2C9E3E4A290972 CRC64;
     MFEFRILKRS KKSRARLGVI STPHGEIETP AFVTVATRAT VRTLESDEVA AAGSQVLICN
     TYHLHTAPGE KNVKRAGGLH EFMQWKRPLM TDSGGFQVFS LGFGKDHGVG KILKEEQERR
     IPEGTQPTHI KITDDGVHFR SPIDGTELFL NPKESIRIQE ALGADIMFAF DECPSPLADE
     DYLRTSLDRT HRWAAQCLKV RKTSQALYGI VQGGCFKNMR IESARLIGAL PFEGFGIGGE
     FGYDKRSLKK MLEHVHDELP ENKPRHVLGV GHPEDFPYIA SAGGDTFDCI APTHYARRGT
     VFTSKGRFQI RNQRYLTDQR PLDPSCKCDI CKTYSRAYIS HLMRAYELTG MKLVSFHNLH
     FFNAQASLLR KRIKNGEI
//
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