TGT_POLNA
ID TGT_POLNA Reviewed; 387 AA.
AC A1VJ15;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=Pnap_0320;
OS Polaromonas naphthalenivorans (strain CJ2).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=365044;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ2;
RX PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT tar-contaminated sediment, reveals physiological and metabolic versatility
RT and evolution through extensive horizontal gene transfer.";
RL Environ. Microbiol. 11:2253-2270(2009).
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; CP000529; ABM35643.1; -; Genomic_DNA.
DR RefSeq; WP_011799750.1; NC_008781.1.
DR AlphaFoldDB; A1VJ15; -.
DR SMR; A1VJ15; -.
DR STRING; 365044.Pnap_0320; -.
DR EnsemblBacteria; ABM35643; ABM35643; Pnap_0320.
DR KEGG; pna:Pnap_0320; -.
DR eggNOG; COG0343; Bacteria.
DR HOGENOM; CLU_022060_0_1_4; -.
DR OMA; GIDLFDC; -.
DR OrthoDB; 1165356at2; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000000644; 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..387
FT /note="Queuine tRNA-ribosyltransferase"
FT /id="PRO_1000058284"
FT REGION 263..269
FT /note="RNA binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT REGION 287..291
FT /note="RNA binding; important for wobble base 34
FT recognition"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT ACT_SITE 102
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT ACT_SITE 282
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 102..106
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
SQ SEQUENCE 387 AA; 43469 MW; CEAB44E249192F8F CRC64;
MLEFEVLKTD PATVDSEGAY LGSYARRGQL TLNHGVVQTP IFMPVGTYGT VKGVTPQSLH
DMNAQIILGN TFHLWMRPGL DVVAQFGGLH KFESWHKPIL TDSGGFQVWS LGEMRKISEE
GVKFASPVNG DKLFLTPEIS MQIQTLLNSD IVMQFDECTP YDTKGHITTE GEARSSMELS
RRWAKRCEIE FDKLENPNAL FGIVQGGMFE NLRQESLDAL VEMDFPGYAV GGVSVGEPKE
EMLRIMAHTP HRLPAHKPRY LMGVGTPEDL VEGVASGVDM FDCVMPTRNA RNGHMFTRFG
DLKIRNARYK SEEAPVDSTC GCYTCRNFSR AYMHHLDRCG EMLGPMLSSI HNLHYYLNLM
QEVRGALDAG RFGEFVRQFK ADRQRGV
