TGT_SYNFM
ID TGT_SYNFM Reviewed; 373 AA.
AC A0LFR2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=Sfum_0565;
OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC Syntrophobacteraceae; Syntrophobacter.
OX NCBI_TaxID=335543;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10017 / MPOB;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL Submitted (OCT-2006) 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; CP000478; ABK16264.1; -; Genomic_DNA.
DR RefSeq; WP_011697437.1; NC_008554.1.
DR AlphaFoldDB; A0LFR2; -.
DR SMR; A0LFR2; -.
DR STRING; 335543.Sfum_0565; -.
DR EnsemblBacteria; ABK16264; ABK16264; Sfum_0565.
DR KEGG; sfu:Sfum_0565; -.
DR eggNOG; COG0343; Bacteria.
DR HOGENOM; CLU_022060_0_1_7; -.
DR OMA; GIDLFDC; -.
DR OrthoDB; 1165356at2; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000001784; 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..373
FT /note="Queuine tRNA-ribosyltransferase"
FT /id="PRO_1000016880"
FT REGION 245..251
FT /note="RNA binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT REGION 269..273
FT /note="RNA binding; important for wobble base 34
FT recognition"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT ACT_SITE 91
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT ACT_SITE 264
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 91..95
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 304
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 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
SQ SEQUENCE 373 AA; 42122 MW; 0A72AFB3655E57A4 CRC64;
MDFRIIARDA SCHARRGRLR TAHGTFDTPV FMPVGTQASV KSLSPDELED LGAHIILGNT
YHLLLRPGAE RVARLGGLHR FMHWNRSILT DSGGFQVFSL ARINRIEEDG VVFQSHIDGA
RHAITPETSM ECQMQLGSDI AMCFDECTAY PVTYEYARES MLRTVRWAAR SKEAHTLPEQ
SLFGIVQGGV FCDLRRDCLE RLVETGFDGY ALGSLSVGES KEEMLSVLEA VAPGLPAASP
RYVMGVGTPE DLVEGVRCGV DMFDCVMPTR NARNGMLFTV RGGIQIKNSR YADDDRPIEE
GCSCYTCRRF SRAYLRHLFL ARELLAYRLN TLHNLHYYLG LMAAMREAIE ANAFDRWRRS
FYLDRENREP AEE
