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TGT_VESOH
ID   TGT_VESOH               Reviewed;         370 AA.
AC   A5CW46;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Queuine tRNA-ribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00168};
DE            EC=2.4.2.29 {ECO:0000255|HAMAP-Rule:MF_00168};
DE   AltName: Full=Guanine insertion enzyme {ECO:0000255|HAMAP-Rule:MF_00168};
DE   AltName: Full=tRNA-guanine transglycosylase {ECO:0000255|HAMAP-Rule:MF_00168};
GN   Name=tgt {ECO:0000255|HAMAP-Rule:MF_00168}; OrderedLocusNames=COSY_0724;
OS   Vesicomyosocius okutanii subsp. Calyptogena okutanii (strain HA).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; sulfur-oxidizing symbionts;
OC   Candidatus Vesicomyosocius.
OX   NCBI_TaxID=412965;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HA;
RX   PubMed=17493812; DOI=10.1016/j.cub.2007.04.039;
RA   Kuwahara H., Yoshida T., Takaki Y., Shimamura S., Nishi S., Harada M.,
RA   Matsuyama K., Takishita K., Kawato M., Uematsu K., Fujiwara Y., Sato T.,
RA   Kato C., Kitagawa M., Kato I., Maruyama T.;
RT   "Reduced genome of the thioautotrophic intracellular symbiont in a deep-sea
RT   clam, Calyptogena okutanii.";
RL   Curr. Biol. 17:881-886(2007).
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:0000255|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:0000255|HAMAP-
CC         Rule:MF_00168};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00168};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00168};
CC   -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC       {ECO:0000255|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:0000255|HAMAP-Rule:MF_00168}.
CC   -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00168}.
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DR   EMBL; AP009247; BAF61836.1; -; Genomic_DNA.
DR   RefSeq; WP_011930106.1; NC_009465.1.
DR   AlphaFoldDB; A5CW46; -.
DR   SMR; A5CW46; -.
DR   STRING; 412965.COSY_0724; -.
DR   EnsemblBacteria; BAF61836; BAF61836; COSY_0724.
DR   KEGG; vok:COSY_0724; -.
DR   eggNOG; COG0343; Bacteria.
DR   HOGENOM; CLU_022060_0_1_6; -.
DR   OMA; GIDLFDC; -.
DR   OrthoDB; 1165356at2; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000000247; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008479; F:queuine tRNA-ribosyltransferase 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; -; 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   Pfam; PF01702; TGT; 1.
DR   SUPFAM; SSF51713; SSF51713; 1.
DR   TIGRFAMs; TIGR00430; Q_tRNA_tgt; 1.
DR   TIGRFAMs; TIGR00449; tgt_general; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Metal-binding; Queuosine biosynthesis; Transferase;
KW   tRNA processing; Zinc.
FT   CHAIN           1..370
FT                   /note="Queuine tRNA-ribosyltransferase"
FT                   /id="PRO_1000058290"
FT   REGION          245..251
FT                   /note="RNA binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT   REGION          269..273
FT                   /note="RNA binding; important for wobble base 34
FT                   recognition"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT   ACT_SITE        89
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT   ACT_SITE        264
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT   BINDING         89..93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT   BINDING         187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT   BINDING         214
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT   BINDING         302
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT   BINDING         304
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT   BINDING         307
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT   BINDING         333
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
SQ   SEQUENCE   370 AA;  42121 MW;  9A88CC349E2FE3B7 CRC64;
     MKFELKNTNY LARRGKIIFD RGEVETPSFM PVGTYGSVKA MTPEELSSFG TQMILGNSFH
     LAITPGIDVV QAHGNLHDFM HWKGPILTDS GGFQVFSLGE TRKISEKGVD FRSPKDGAKI
     FMGPEESIQI QKKLGSDIVM IFDECTPYPA DKKTVYKSMQ LSLRWAQRSK NEHDRLNNKN
     ALFGIVQGGM HEDLRIQSAA TLVEIGFNGF AIGGLSVGES KEEMIKVLDY LPSQLPSDKL
     RYLMGVGTPK DLVEAVERGI DMFDCVMPTR NARNGYLFTS IGIVKIRNAR YRLDTSVLDE
     CCHCYTCQNY SKSYLHHLQR KNEILGARLN TIHNLYYYQY LMLQMRRAIE SNKFSKFKKE
     FYQQQGHDTL
 
 
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