TGT_SYNE7
ID TGT_SYNE7 Reviewed; 384 AA.
AC Q8GAA6; Q31R32;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 95.
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};
GN OrderedLocusNames=Synpcc7942_0455; ORFNames=sel0015;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Holtman C.K., Sandoval P., Chen Y., Socias T., Mohler B.J., McMurtry S.,
RA Gonzalez A., Salinas I., Golden S.S., Youderian P.;
RT "Synechococcus elongatus PCC 7942 cosmid 3E9.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD55621.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X04616; CAD55621.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP000100; ABB56487.1; -; Genomic_DNA.
DR RefSeq; WP_011377585.1; NC_007604.1.
DR AlphaFoldDB; Q8GAA6; -.
DR SMR; Q8GAA6; -.
DR STRING; 1140.Synpcc7942_0455; -.
DR PRIDE; Q8GAA6; -.
DR EnsemblBacteria; ABB56487; ABB56487; Synpcc7942_0455.
DR KEGG; syf:Synpcc7942_0455; -.
DR eggNOG; COG0343; Bacteria.
DR HOGENOM; CLU_022060_0_1_3; -.
DR OMA; GIDLFDC; -.
DR OrthoDB; 1165356at2; -.
DR BioCyc; SYNEL:SYNPCC7942_0455-MON; -.
DR UniPathway; UPA00392; -.
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; Transferase;
KW tRNA processing; Zinc.
FT CHAIN 1..384
FT /note="Queuine tRNA-ribosyltransferase"
FT /id="PRO_0000135542"
FT REGION 258..264
FT /note="RNA binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT REGION 282..286
FT /note="RNA binding; important for wobble base 34
FT recognition"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT ACT_SITE 103
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT ACT_SITE 277
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 103..107
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT BINDING 317
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
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 346
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
SQ SEQUENCE 384 AA; 43093 MW; 8325FF44311F5E82 CRC64;
MDRQCAVASL TAFQFQIDRQ CSQTRGRACS FHTPHGIVET PRFMPVGTLA TVKTVTPAQL
RDTGAQMVLS NTYHLHLQPG EEIVAKAGGL HRFMNWSGPM LTDSGGFQVF SLSELRKIEE
RGVTFRSPRD GAVIEFTPER SIRIQNALGA DVIMAFDECP PYPAERKDVE AAVARTYRWL
ERCINAHERP QDQALFGIVQ GGVYLDLRQQ AARDLVQLDL PGYAIGGVSV GEPSEEIHRI
VEATAPLLPA HKPRYLMGVG TYREMVQAIA AGIDLFDCVI PTRLARHGAA LVKGDRWNLK
NAQFREDFQP LDEDCNCYCC QNFSRAYLNH LIRSREILGY TLLSIHNITE LVRFTTRIRE
AILSDRFVEE FGHWLQPSAV PVSP
