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Database: UniProt
Entry: A0A193GIF4_9BORD
LinkDB: A0A193GIF4_9BORD
Original site: A0A193GIF4_9BORD 
ID   A0A193GIF4_9BORD        Unreviewed;       392 AA.
AC   A0A193GIF4;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 39.
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=BAU07_21600 {ECO:0000313|EMBL:ANN79373.1};
OS   Bordetella flabilis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=463014 {ECO:0000313|EMBL:ANN79373.1, ECO:0000313|Proteomes:UP000091926};
RN   [1] {ECO:0000313|EMBL:ANN79373.1, ECO:0000313|Proteomes:UP000091926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU10664 {ECO:0000313|EMBL:ANN79373.1,
RC   ECO:0000313|Proteomes:UP000091926};
RA   LiPuma J.J., Spilker T.;
RT   "Complete genome sequences of Bordetella bronchialis and Bordetella
RT   flabilis.";
RL   Submitted (JUN-2016) 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}.
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DR   EMBL; CP016172; ANN79373.1; -; Genomic_DNA.
DR   RefSeq; WP_066662321.1; NZ_CP016172.1.
DR   AlphaFoldDB; A0A193GIF4; -.
DR   STRING; 463014.BAU07_21600; -.
DR   KEGG; bfz:BAU07_21600; -.
DR   OrthoDB; 9805417at2; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000091926; Chromosome.
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          13..373
FT                   /note="tRNA-guanine(15) transglycosylase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01702"
FT   REGION          253..259
FT                   /note="RNA binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   REGION          277..281
FT                   /note="RNA binding; important for wobble base 34
FT                   recognition"
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        272
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         146
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   BINDING         195
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   BINDING         222
FT                   /ligand="substrate"
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         312
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   BINDING         315
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   BINDING         341
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
SQ   SEQUENCE   392 AA;  43441 MW;  AE9803ECBC3EBB78 CRC64;
     MTGLHFELLA TDGAARRGRI TLNHGVVETP IFMPVGTYGS VKAMLPHELD EVGAQIVLGN
     TFHLWLRPGT DIMEKHGGLH GFMGWNRPIL TDSGGFQVFS LQGMRKITEE GVRFASPIDG
     ARLFLTPEES MRIQRALNSD IVMVFDECTP YEIDGRAATE EEAARSMRMS LRWARRSRDA
     FDGLGNPNAL FGIVQGGMYE RLRDESLAGL QDIGFHGYAI GGLSVGEPKE DMMRILGHVA
     PRLPAQAPRY LMGVGTPEDL VAGVAQGIDM FDCVMPTRNA RNGWLFTRYG DIKIRNARYR
     DDTRPLDGSC ACHTCRLFTR AYLHHLQRAN EITGARLNTL HNLHFYLALM AEMRDAIAAG
     RFEAWRARFA ADRARGVDQG GAGRHGDNPG TP
//
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