ID Q4FLZ2_PELUB Unreviewed; 370 AA.
AC Q4FLZ2;
DT 30-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 134.
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:AAZ21796.1};
GN OrderedLocusNames=SAR11_0988 {ECO:0000313|EMBL:AAZ21796.1};
OS Pelagibacter ubique (strain HTCC1062).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC Candidatus Pelagibacteraceae; Pelagibacter.
OX NCBI_TaxID=335992 {ECO:0000313|EMBL:AAZ21796.1, ECO:0000313|Proteomes:UP000002528};
RN [1] {ECO:0000313|EMBL:AAZ21796.1, ECO:0000313|Proteomes:UP000002528}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC1062 {ECO:0000313|EMBL:AAZ21796.1,
RC ECO:0000313|Proteomes:UP000002528};
RX PubMed=16109880; DOI=10.1126/science.1114057;
RA Giovannoni S.J., Tripp H.J., Givan S., Podar M., Vergin K.L., Baptista D.,
RA Bibbs L., Eads J., Richardson T.H., Noordewier M., Rappe M.S., Short J.M.,
RA Carrington J.C., Mathur E.J.;
RT "Genome streamlining in a cosmopolitan oceanic bacterium.";
RL Science 309:1242-1245(2005).
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; CP000084; AAZ21796.1; -; Genomic_DNA.
DR RefSeq; WP_011282087.1; NC_007205.1.
DR AlphaFoldDB; Q4FLZ2; -.
DR STRING; 335992.SAR11_0988; -.
DR KEGG; pub:SAR11_0988; -.
DR eggNOG; COG0343; Bacteria.
DR HOGENOM; CLU_022060_0_1_5; -.
DR OrthoDB; 9805417at2; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000002528; Chromosome.
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:UP000002528};
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 17..369
FT /note="tRNA-guanine(15) transglycosylase-like"
FT /evidence="ECO:0000259|Pfam:PF01702"
FT REGION 250..256
FT /note="RNA binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT REGION 274..278
FT /note="RNA binding; important for wobble base 34
FT recognition"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT ACT_SITE 94
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT ACT_SITE 269
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT BINDING 94..98
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
SQ SEQUENCE 370 AA; 41502 MW; FC9DB2E4AA3DE235 CRC64;
MALKNFKFNV IESNKFARVG VIETHRGNIQ TPAFMPVGTQ ATVKACLIDD VIKTGSEIIL
SNTYHLMIRP GVDRIISAGG LHKFMNCKLP ILTDSGGFQV MSLSKLNKVD REKGAIFNSH
VDGKKFILSP EESIRVQKGL DSDIVMIMDE CPKKTTDYKV INKSMELSIY WAERSKIAFG
LNPHKALFGI IQGGLFKDLR TKSLNNLIKI GFDGYAIGGL AVGESQNEMF SVLDDLKNIM
PDDKPRYLMG VGTPADILGA VKRGVDMFDC VMPTRSGRTG LAFTWNGRVN IKNNKYKNDN
EPLDPNCSNL NLNKYSKNYI NHLFNTNEIL GSTLLTLHNI NFYQELMSSI RENIKKGTFD
KFHDEYIDKL
//
