TGT_THEMA
ID TGT_THEMA Reviewed; 369 AA.
AC Q9X1P7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 132.
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=TM_1561;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ZINC.
RG Joint Center for Structural Genomics (JCSG);
RT "Crystal structure of queuine tRNA-ribosyltransferase (EC 2.4.2.29) (tRNA-
RT guanine (tm1561) from Thermotoga maritima at 1.90 A resolution.";
RL Submitted (AUG-2005) to the PDB data bank.
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; AE000512; AAD36627.1; -; Genomic_DNA.
DR PIR; D72240; D72240.
DR RefSeq; NP_229361.1; NC_000853.1.
DR RefSeq; WP_004081969.1; NZ_CP011107.1.
DR PDB; 2ASH; X-ray; 1.90 A; A/B/C/D=1-369.
DR PDBsum; 2ASH; -.
DR AlphaFoldDB; Q9X1P7; -.
DR SMR; Q9X1P7; -.
DR STRING; 243274.THEMA_06475; -.
DR EnsemblBacteria; AAD36627; AAD36627; TM_1561.
DR KEGG; tma:TM1561; -.
DR KEGG; tmw:THMA_1596; -.
DR PATRIC; fig|243274.18.peg.1249; -.
DR eggNOG; COG0343; Bacteria.
DR InParanoid; Q9X1P7; -.
DR OMA; GIDLFDC; -.
DR OrthoDB; 1165356at2; -.
DR UniPathway; UPA00392; -.
DR EvolutionaryTrace; Q9X1P7; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0002099; P:tRNA wobble guanine modification; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; Metal-binding; Queuosine biosynthesis;
KW Reference proteome; Transferase; tRNA processing; Zinc.
FT CHAIN 1..369
FT /note="Queuine tRNA-ribosyltransferase"
FT /id="PRO_0000135545"
FT REGION 242..248
FT /note="RNA binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT REGION 266..270
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 261
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 142
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 211
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168,
FT ECO:0000269|Ref.2"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168,
FT ECO:0000269|Ref.2"
FT BINDING 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168,
FT ECO:0000269|Ref.2"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168,
FT ECO:0000269|Ref.2"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:2ASH"
FT STRAND 12..19
FT /evidence="ECO:0007829|PDB:2ASH"
FT STRAND 22..37
FT /evidence="ECO:0007829|PDB:2ASH"
FT HELIX 43..49
FT /evidence="ECO:0007829|PDB:2ASH"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:2ASH"
FT HELIX 59..63
FT /evidence="ECO:0007829|PDB:2ASH"
FT HELIX 67..72
FT /evidence="ECO:0007829|PDB:2ASH"
FT HELIX 76..80
FT /evidence="ECO:0007829|PDB:2ASH"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:2ASH"
FT HELIX 92..96
FT /evidence="ECO:0007829|PDB:2ASH"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:2ASH"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:2ASH"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:2ASH"
FT HELIX 123..133
FT /evidence="ECO:0007829|PDB:2ASH"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:2ASH"
FT HELIX 151..171
FT /evidence="ECO:0007829|PDB:2ASH"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:2ASH"
FT HELIX 189..200
FT /evidence="ECO:0007829|PDB:2ASH"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:2ASH"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:2ASH"
FT HELIX 218..229
FT /evidence="ECO:0007829|PDB:2ASH"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:2ASH"
FT HELIX 246..253
FT /evidence="ECO:0007829|PDB:2ASH"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:2ASH"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:2ASH"
FT HELIX 264..270
FT /evidence="ECO:0007829|PDB:2ASH"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:2ASH"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:2ASH"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:2ASH"
FT HELIX 302..306
FT /evidence="ECO:0007829|PDB:2ASH"
FT HELIX 309..317
FT /evidence="ECO:0007829|PDB:2ASH"
FT HELIX 321..347
FT /evidence="ECO:0007829|PDB:2ASH"
FT HELIX 351..361
FT /evidence="ECO:0007829|PDB:2ASH"
SQ SEQUENCE 369 AA; 41429 MW; 5E9FF9C589347DF2 CRC64;
MEFEVKKTFG KARLGVMKLH HGAVETPVFM PVGTNASVKL LTPRDLEEAG AEIILSNTFH
LMLKPGVEII KLHRGLHNFM GWKRPILTDS GGFQVFSLPK IRIDDEGVVF RSPIDGSKVF
LNPEISMEVQ IALGSDICMV FDHCPVPDAD YEEVKEATER TYRWALRSKK AFKTENQALF
GIVQGGIYPD LRRESALQLT SIGFDGYAIG GLSIGEERSL TLEMTEVTVE FLPEDKPRYF
MGGGSPELIL ELVDRGVDMF DSVFPTRIAR HGTALTWNGK LNLKASYNKR SLEPVDERCG
CYTCKNFTRS YIHHLFDRGE VLGQILLTIH NINFMISLMK EVRRSIESGT FKELKSKVVE
VYSSGGVNV
