TGT_DINSH
ID TGT_DINSH Reviewed; 376 AA.
AC A8LRQ1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=Dshi_2346;
OS Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Dinoroseobacter.
OX NCBI_TaxID=398580;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16493 / NCIMB 14021 / DFL 12;
RX PubMed=19741735; DOI=10.1038/ismej.2009.94;
RA Wagner-Dobler I., Ballhausen B., Berger M., Brinkhoff T., Buchholz I.,
RA Bunk B., Cypionka H., Daniel R., Drepper T., Gerdts G., Hahnke S., Han C.,
RA Jahn D., Kalhoefer D., Kiss H., Klenk H.P., Kyrpides N., Liebl W.,
RA Liesegang H., Meincke L., Pati A., Petersen J., Piekarski T.,
RA Pommerenke C., Pradella S., Pukall R., Rabus R., Stackebrandt E., Thole S.,
RA Thompson L., Tielen P., Tomasch J., von Jan M., Wanphrut N., Wichels A.,
RA Zech H., Simon M.;
RT "The complete genome sequence of the algal symbiont Dinoroseobacter shibae:
RT a hitchhiker's guide to life in the sea.";
RL ISME J. 4:61-77(2010).
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; CP000830; ABV94082.1; -; Genomic_DNA.
DR RefSeq; WP_012179013.1; NC_009952.1.
DR AlphaFoldDB; A8LRQ1; -.
DR SMR; A8LRQ1; -.
DR STRING; 398580.Dshi_2346; -.
DR EnsemblBacteria; ABV94082; ABV94082; Dshi_2346.
DR KEGG; dsh:Dshi_2346; -.
DR eggNOG; COG0343; Bacteria.
DR HOGENOM; CLU_022060_0_1_5; -.
DR OMA; GIDLFDC; -.
DR OrthoDB; 1165356at2; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000006833; 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; Zinc.
FT CHAIN 1..376
FT /note="Queuine tRNA-ribosyltransferase"
FT /id="PRO_1000077007"
FT REGION 248..254
FT /note="RNA binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT ACT_SITE 93
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT ACT_SITE 267
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 93..97
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 305
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 310
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 336
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
SQ SEQUENCE 376 AA; 41607 MW; 4A735F7E600BE3A3 CRC64;
MTQRFSFTRL GQDGAARLGR INTPRGEIRT PAFMPVGTAA TVKAMRPESV RETGADILLG
NTYHLMLRPT AERIARLGGL HRFMNWDRPI LTDSGGFQVM SLTGLRKLTE QGVTFKSHID
GSKHMLSPER SMEIQKLLRS DIVMCFDECP ALPAPRERIT ESMELSMRWA ARSREAFGDW
PGHALFGIQQ GGLEEDLRGK SAEALRAIEF DGYAVGGLAV GEGQEAMFGV LDYAPGMLPE
DKPRYLMGVG KPGDLVGAVK RGIDMFDCVL PSRSGRTGQV FTRRGVVNIK NARHADDPRP
LDEDCTCPAC RSYSRAYLHH VFRAGEILSS MLLTWHNLHY YQELMQGMRD AIGAGDFAGF
EARFLAQQAE GDIAPV
