ID F4LTJ4_TEPAE Unreviewed; 372 AA.
AC F4LTJ4; L0S2I1;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Queuine tRNA-ribosyltransferase {ECO:0000256|HAMAP-Rule:MF_00168};
DE EC=2.4.2.29 {ECO:0000256|HAMAP-Rule:MF_00168};
DE AltName: Full=Guanine insertion enzyme {ECO:0000256|HAMAP-Rule:MF_00168};
DE AltName: Full=tRNA-guanine transglycosylase {ECO:0000256|HAMAP-Rule:MF_00168};
GN Name=tgt {ECO:0000256|HAMAP-Rule:MF_00168,
GN ECO:0000313|EMBL:CCP26012.1};
GN OrderedLocusNames=TEPIRE1_1288 {ECO:0000313|EMBL:CCP26012.1};
OS Tepidanaerobacter acetatoxydans (strain DSM 21804 / JCM 16047 / Re1).
OC Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC Tepidanaerobacteraceae; Tepidanaerobacter.
OX NCBI_TaxID=1209989 {ECO:0000313|EMBL:CCP26012.1, ECO:0000313|Proteomes:UP000010802};
RN [1] {ECO:0000313|Proteomes:UP000010802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Re1 {ECO:0000313|Proteomes:UP000010802};
RX PubMed=23469343; DOI=10.1128/genomeA.00213-12;
RA Manzoor S., Bongcam-Rudloff E., Schnurer A., Muller B.;
RT "First genome sequence of a syntrophic acetate-oxidizing bacterium,
RT Tepidanaerobacter acetatoxydans strain Re1.";
RL Genome Announc. 1:E00213-E00213(2013).
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:0000256|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:0000256|HAMAP-
CC Rule:MF_00168};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00168};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00168};
CC -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_00168}.
CC -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.
CC {ECO:0000256|HAMAP-Rule:MF_00168}.
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DR EMBL; HF563609; CCP26012.1; -; Genomic_DNA.
DR RefSeq; WP_013778247.1; NC_019954.2.
DR AlphaFoldDB; F4LTJ4; -.
DR STRING; 1209989.TepRe1_1178; -.
DR KEGG; tae:TepiRe1_1288; -.
DR KEGG; tep:TepRe1_1178; -.
DR PATRIC; fig|1209989.3.peg.1425; -.
DR eggNOG; COG0343; Bacteria.
DR HOGENOM; CLU_022060_0_1_9; -.
DR OrthoDB; 9805417at2; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000010802; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008479; F:tRNA-guanosine(34) queuine transglycosylase 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; Queuine tRNA-ribosyltransferase-like; 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 NCBIfam; TIGR00430; Q_tRNA_tgt; 1.
DR NCBIfam; TIGR00449; tgt_general; 1.
DR PANTHER; PTHR46499; QUEUINE TRNA-RIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR46499:SF1; QUEUINE TRNA-RIBOSYLTRANSFERASE; 1.
DR Pfam; PF01702; TGT; 1.
DR SUPFAM; SSF51713; tRNA-guanine transglycosylase; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_00168}; Metal-binding {ECO:0000256|HAMAP-Rule:MF_00168};
KW Queuosine biosynthesis {ECO:0000256|ARBA:ARBA00022785, ECO:0000256|HAMAP-
KW Rule:MF_00168}; Reference proteome {ECO:0000313|Proteomes:UP000010802};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00168};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00168}; Zinc {ECO:0000256|HAMAP-Rule:MF_00168}.
FT DOMAIN 13..365
FT /note="tRNA-guanine(15) transglycosylase-like"
FT /evidence="ECO:0000259|Pfam:PF01702"
FT REGION 246..252
FT /note="RNA binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT REGION 270..274
FT /note="RNA binding; important for wobble base 34
FT recognition"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT ACT_SITE 91
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT ACT_SITE 265
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT BINDING 91..95
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT BINDING 308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT BINDING 334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
SQ SEQUENCE 372 AA; 41772 MW; 9D56175B8F41ADD8 CRC64;
MNFNILKKSA NTSARLGELE TLHGSFATPV FMPVGTQATV KTMTPDELKE IGAKIILSNT
YHLYLRPGHE IIREAGGLHK FMNWDGSILT DSGGFQVFSL GELREINEEG VTFRSHIDGS
IHFIGPETSV EIQNALGSDI MMAFDECIPY PATFEYVLSS VERTTRWAER CQKAHNNIDT
QTLFGIVQGG VYKELRRKSA IDIVSLGFEG YAIGGLSVGE PKKEMYDMLD FTVPLLPDDK
PRYLMGVGTP EDLFEGVIRG IDMFDCVLPT RIARHGTVFT KKGKLVVRNA AYARDFTPLD
PSCDCYACKN FTRAYIRHLI NVGEILGIRL TTIHNLHFLV TLMQEIQKAI EGDYLLELKD
EFYANFGILQ YM
//
