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Database: UniProt
Entry: A0A0C2BT52_9BURK
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ID   A0A0C2BT52_9BURK        Unreviewed;       375 AA.
AC   A0A0C2BT52;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 46.
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=TSA66_11045 {ECO:0000313|EMBL:KIF81236.1};
OS   Noviherbaspirillum autotrophicum.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Noviherbaspirillum.
OX   NCBI_TaxID=709839 {ECO:0000313|EMBL:KIF81236.1, ECO:0000313|Proteomes:UP000031572};
RN   [1] {ECO:0000313|EMBL:KIF81236.1, ECO:0000313|Proteomes:UP000031572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSA66 {ECO:0000313|EMBL:KIF81236.1,
RC   ECO:0000313|Proteomes:UP000031572};
RA   Ishii S., Ashida N., Ohno H., Otsuka S., Yokota A., Senoo K.;
RT   "Denitrispirillum autotrophicum gen. nov., sp. nov., Denitrifying,
RT   Facultatively Autotrophic Bacteria Isolated from Rice Paddy Soil.";
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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: 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:KIF81236.1}.
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DR   EMBL; JWJG01000028; KIF81236.1; -; Genomic_DNA.
DR   RefSeq; WP_040040061.1; NZ_JWJG01000028.1.
DR   AlphaFoldDB; A0A0C2BT52; -.
DR   STRING; 709839.TSA66_11045; -.
DR   OrthoDB; 9805417at2; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000031572; 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   Reference proteome {ECO:0000313|Proteomes:UP000031572};
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          11..371
FT                   /note="tRNA-guanine(15) transglycosylase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01702"
FT   REGION          251..257
FT                   /note="RNA binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   REGION          275..279
FT                   /note="RNA binding; important for wobble base 34
FT                   recognition"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   ACT_SITE        90
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   ACT_SITE        270
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   BINDING         90..94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   BINDING         144
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   BINDING         193
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   BINDING         220
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   BINDING         308
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   BINDING         310
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   BINDING         313
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   BINDING         339
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
SQ   SEQUENCE   375 AA;  42186 MW;  17BF1D0B0320A409 CRC64;
     MLNFKLIKTD GHARRGRLTL NHGVVETPIF MPVGTYGSVK AMSPLELHDI DAQIILGNTF
     HLWLRPGLDV ISKFDGLHRF IGWNKPVLTD SGGFQVFSLG AMRKITEEGV KFASPINGDK
     LFLSPEISMQ IQRVLNSDIV MQFDECTPYE IEGRPATEAE AAKSMRMSLR WAKRSRDEFD
     RGENPNALFG IVQGGMFEHL RDESLAGLQE IGFGGIAIGG LSVGEPKEDM MRVLAHVGPR
     LPADKPHYLM GVGTPEDLVA GVANGVDMFD CVMPTRNARN GWLFTRFGDL KIKNARYKDD
     EKPLDETCEC YACRNFSRAY LYHLHRAGEI LGARLNTIHN LHYYLQLMRE MRAAIDNDRF
     QAFVVQFHAD RARGV
//
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