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TGT_SHIFL
ID   TGT_SHIFL               Reviewed;         375 AA.
AC   Q54177;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 148.
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}; Synonyms=vacC;
GN   OrderedLocusNames=SF0343, S0351;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=YSH6000 / Serotype 2a;
RX   PubMed=8045893; DOI=10.1128/jb.176.15.4627-4634.1994;
RA   Durand J.M., Okada N., Tobe T., Watarai M., Fukuda I., Suzuki T.,
RA   Nakata N., Komatsu K., Yoshikawa M., Sasakawa C.;
RT   "vacC, a virulence-associated chromosomal locus of Shigella flexneri, is
RT   homologous to tgt, a gene encoding tRNA-guanine transglycosylase (Tgt) of
RT   Escherichia coli K-12.";
RL   J. Bacteriol. 176:4627-4634(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
CC   -!- FUNCTION: Important for virulence.
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; D26469; BAA05482.1; -; Genomic_DNA.
DR   EMBL; AE005674; AAN42001.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP15878.1; -; Genomic_DNA.
DR   RefSeq; NP_706294.1; NC_004337.2.
DR   RefSeq; WP_000667315.1; NZ_WPGW01000023.1.
DR   AlphaFoldDB; Q54177; -.
DR   SMR; Q54177; -.
DR   STRING; 198214.SF0343; -.
DR   EnsemblBacteria; AAN42001; AAN42001; SF0343.
DR   EnsemblBacteria; AAP15878; AAP15878; S0351.
DR   GeneID; 1027667; -.
DR   GeneID; 58389236; -.
DR   KEGG; sfl:SF0343; -.
DR   KEGG; sfx:S0351; -.
DR   PATRIC; fig|198214.7.peg.394; -.
DR   HOGENOM; CLU_022060_0_1_6; -.
DR   OMA; GIDLFDC; -.
DR   OrthoDB; 1165356at2; -.
DR   BRENDA; 2.4.2.29; 5712.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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;
KW   Reference proteome; Transferase; tRNA processing; Virulence; Zinc.
FT   CHAIN           1..375
FT                   /note="Queuine tRNA-ribosyltransferase"
FT                   /id="PRO_0000135520"
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   375 AA;  42608 MW;  52BA93AD0F170720 CRC64;
     MKFELDTTDG RARRGRLVFD RGVVETPCFM PVGTYGTVKG MTPEEVEATG AQIILGNTFH
     LWLRPGQEIM KLHGDLHDFM QWKGPILTDS GGFQVFSLGD IRKITEQGVH FRNPINGDPI
     FLDPEKSMEI QYDLGSDIVM IFDECTPYPA DWDYAKRSME MSLRWAKRSR ERFDSLGNKN
     ALFGIIQGSI YEDLRDISVK GLVDIGFDGY AVGGLAVGEP KADMHRILEH VCPQIPADKP
     RYLMGVGKPE DLVEGVRRGI DMFDCVMPTR NARNGHLFVT DGVVKIRNAK YKSDTGPLDP
     ECDCYTCRNY SRAYLHHLDR CNEILGARLN TIHNLRYYQR LMAGLRKAIE EGKLESFVTD
     FYQRQGREVP PLNVD
 
 
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