TGT_HELHP
ID TGT_HELHP Reviewed; 381 AA.
AC Q7VHX2;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=HH_0841;
OS Helicobacter hepaticus (strain ATCC 51449 / 3B1).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=235279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51449 / 3B1;
RX PubMed=12810954; DOI=10.1073/pnas.1332093100;
RA Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., Bell M.,
RA Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A., Holland R.,
RA Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G., Schauer D.B.,
RA Shen Z., Weber J., Frosch M., Fox J.G.;
RT "The complete genome sequence of the carcinogenic bacterium Helicobacter
RT hepaticus.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(2003).
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; AE017125; AAP77438.1; -; Genomic_DNA.
DR RefSeq; WP_011115681.1; NC_004917.1.
DR AlphaFoldDB; Q7VHX2; -.
DR SMR; Q7VHX2; -.
DR STRING; 235279.HH_0841; -.
DR EnsemblBacteria; AAP77438; AAP77438; HH_0841.
DR KEGG; hhe:HH_0841; -.
DR eggNOG; COG0343; Bacteria.
DR HOGENOM; CLU_022060_0_1_7; -.
DR OMA; GIDLFDC; -.
DR OrthoDB; 1165356at2; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000002495; 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..381
FT /note="Queuine tRNA-ribosyltransferase"
FT /id="PRO_0000135482"
FT REGION 252..258
FT /note="RNA binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT REGION 276..280
FT /note="RNA binding; important for wobble base 34
FT recognition"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT ACT_SITE 90
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT ACT_SITE 271
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 90..94
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 311
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 314
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
SQ SEQUENCE 381 AA; 42842 MW; D6A4E8E6C2AB824A CRC64;
MQVTLQAQDG GARALSLKLA HSEVQTPVFM PVGTQGCVKA LDSRDMSEIL NAQIILVNTY
HMYLRIGIER LKNFGGIARF AHFDRSYLSD SGGFQAFSLN KNAKVTNEGV AFKSHIDGSK
HFFSPEYVLD IQYALNSDIM MVLDDLVGLP SSEERIADSI ARTSDWAQKS LIYHQSQKAR
GLGLNNNLFA IIQGGVNEHF RTLCAKQLVD MGDFDGFAIG GLAVGETSEQ MYKTISFTTP
LMPVNKPRYL MGVGTPENII ESIALGVDMF DCVMPTRNAR NATLFTHFGK INIKAAIFSN
DQSPIDELCD CYTCQHFTRA YLCHLFRSQE MTYYRLASLH NLHYYLNLMR EAREAILQGT
FSAYRSSFYA LREMEIPNNE Y
