ID A0A1I6RBF6_9SPHI Unreviewed; 376 AA.
AC A0A1I6RBF6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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 ORFNames=SAMN05660206_103327 {ECO:0000313|EMBL:SFS62052.1};
OS Sphingobacterium wenxiniae.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=683125 {ECO:0000313|EMBL:SFS62052.1, ECO:0000313|Proteomes:UP000198785};
RN [1] {ECO:0000313|EMBL:SFS62052.1, ECO:0000313|Proteomes:UP000198785}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22789 {ECO:0000313|EMBL:SFS62052.1,
RC ECO:0000313|Proteomes:UP000198785};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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: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 -!- 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00168}.
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DR EMBL; FOZZ01000003; SFS62052.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6RBF6; -.
DR STRING; 683125.SAMN05660206_103327; -.
DR OrthoDB; 9805417at2; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000198785; Unassembled WGS sequence.
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}; Queuosine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00168};
KW Reference proteome {ECO:0000313|Proteomes:UP000198785};
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}.
FT DOMAIN 13..370
FT /note="tRNA-guanine(15) transglycosylase-like"
FT /evidence="ECO:0000259|Pfam:PF01702"
FT REGION 252..258
FT /note="RNA binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT REGION 276..280
FT /note="RNA binding; important for wobble base 34
FT recognition"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT ACT_SITE 92
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT ACT_SITE 271
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT BINDING 92..96
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
SQ SEQUENCE 376 AA; 42630 MW; 4AB26504CE217496 CRC64;
MKFTLQAQDT GSRARAGVLH TAHGDIQTPI FMPVGTAGTV KAVHQHELVN DIQAQIILGN
TYHLYLRPGL DVLHKAGGLH KFNNWQGPIL TDSGGYQVYS LTEVRKIREE GVTFRSHIDG
SKHLFTPENV MDTQRVIGAD IIMAFDECTP YPCEYSYARK SLDMTHRWLK RCVDRFDSTE
PLYGYEQTLF PIVQGSVYKD LREKSAEVIA SFNRDGNAIG GLSVGEPAEE MYAMTDVVTN
ILPKDKPRYL MGVGTPVNIL ENIALGIDMF DCVMPTRNAR NGMLFTQNGI INIKNEKWKD
DFSPIEAESD LLVDQIHTKA YLRHLIRSQE ILGAQIASLH NLHFYLWLVK QARDKIIEGT
FYTWKEKMIK ILGQRL
//
