TGT_HELPY
ID TGT_HELPY Reviewed; 371 AA.
AC O08314;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 125.
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=HP_0281;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=P1;
RA Bereswill S., Fassbinder F., Voelzing C., Haas R., Kist M.;
RL Submitted (MAR-1997) 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: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; AE000511; AAD07350.1; -; Genomic_DNA.
DR EMBL; Y12061; CAA72784.1; -; Genomic_DNA.
DR PIR; A64555; A64555.
DR RefSeq; NP_207079.1; NC_000915.1.
DR RefSeq; WP_000347385.1; NC_018939.1.
DR AlphaFoldDB; O08314; -.
DR SMR; O08314; -.
DR DIP; DIP-3104N; -.
DR IntAct; O08314; 10.
DR MINT; O08314; -.
DR STRING; 85962.C694_01420; -.
DR PaxDb; O08314; -.
DR EnsemblBacteria; AAD07350; AAD07350; HP_0281.
DR KEGG; hpy:HP_0281; -.
DR PATRIC; fig|85962.47.peg.301; -.
DR eggNOG; COG0343; Bacteria.
DR OMA; GIDLFDC; -.
DR PhylomeDB; O08314; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008479; F:queuine tRNA-ribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0101030; P:tRNA-guanine transglycosylation; IBA:GO_Central.
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..371
FT /note="Queuine tRNA-ribosyltransferase"
FT /id="PRO_0000135483"
FT REGION 246..252
FT /note="RNA binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT REGION 270..274
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="Nucleophile"
FT ACT_SITE 90
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT ACT_SITE 265
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 91
FT /ligand="substrate"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
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 308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT VARIANT 10..11
FT /note="NN -> KH (in strain: P1)"
FT VARIANT 18
FT /note="N -> D (in strain: P1)"
FT VARIANT 46
FT /note="A -> V (in strain: P1)"
FT VARIANT 48
FT /note="E -> G (in strain: P1)"
FT VARIANT 72..73
FT /note="EE -> GQ (in strain: P1)"
FT VARIANT 76
FT /note="G -> V (in strain: P1)"
FT VARIANT 79
FT /note="R -> H (in strain: P1)"
FT VARIANT 84
FT /note="Y -> Q (in strain: P1)"
FT VARIANT 108
FT /note="D -> G (in strain: P1)"
FT VARIANT 119..120
FT /note="SK -> NN (in strain: P1)"
FT VARIANT 169
FT /note="M -> L (in strain: P1)"
FT VARIANT 177
FT /note="K -> N (in strain: P1)"
FT VARIANT 181
FT /note="S -> N (in strain: P1)"
FT VARIANT 206
FT /note="E -> K (in strain: P1)"
FT VARIANT 233
FT /note="A -> T (in strain: P1)"
FT VARIANT 258
FT /note="S -> G (in strain: P1)"
FT VARIANT 304
FT /note="A -> T (in strain: P1)"
SQ SEQUENCE 371 AA; 41416 MW; 2F579B19EA90FD6A CRC64;
MDFQLQATDN NARAGLLNLA HSQVATPVFM PVGTQGCIKS LDATDAQEIL GAKLILANTY
HMYLRPGEKV VEELGGLHRF AQFYGSFLTD SGGFQAFSLS DNVKLQEDGI VFKSHIDGSK
HLFTPAKVLD IQYSLNSDIM MVLDDLVGLP APLKRLEESI KRSAKWANMS LEYHKEKNRP
SNNLFAIIQG GTHLKMRSLS VGLTHEGFDG YAIGGLAVGE SADEMLETIA HTAPLLPKDK
PRYLMGVGTP ENILDAISLG VDMFDCVMPT RNARNATLFT HSGKISIKNA PYKLDNTPIE
ENCACYACKR YSKAYLHHLF RAKELTYARL ASLHNLHFYL ELVKNARNAI LEKRFLSFKK
EFLEKYNSRS H
