ID A0A1R1LLU9_9GAMM Unreviewed; 371 AA.
AC A0A1R1LLU9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=BGP75_21455 {ECO:0000313|EMBL:OMH28464.1};
OS Motiliproteus sp. MSK22-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Motiliproteus.
OX NCBI_TaxID=1897630 {ECO:0000313|EMBL:OMH28464.1, ECO:0000313|Proteomes:UP000187359};
RN [1] {ECO:0000313|EMBL:OMH28464.1, ECO:0000313|Proteomes:UP000187359}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSK22-1 {ECO:0000313|EMBL:OMH28464.1,
RC ECO:0000313|Proteomes:UP000187359};
RA Nakajima Y., Yoshizawa S., Ogura Y., Hayashi T., Kogure K.;
RT "Draft genome of Motiliproteus sp. strain MSK22-1.";
RL Submitted (AUG-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 -!- 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OMH28464.1}.
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DR EMBL; MIEQ01000073; OMH28464.1; -; Genomic_DNA.
DR RefSeq; WP_076720965.1; NZ_MIEQ01000073.1.
DR AlphaFoldDB; A0A1R1LLU9; -.
DR STRING; 1897630.BGP75_21455; -.
DR OrthoDB; 9805417at2; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000187359; Unassembled WGS sequence.
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|HAMAP-Rule:MF_00168};
KW Reference proteome {ECO:0000313|Proteomes:UP000187359};
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 11..364
FT /note="tRNA-guanine(15) transglycosylase-like"
FT /evidence="ECO:0000259|Pfam:PF01702"
FT REGION 243..249
FT /note="RNA binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT REGION 267..271
FT /note="RNA binding; important for wobble base 34
FT recognition"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT ACT_SITE 89
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT ACT_SITE 262
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT BINDING 89..93
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT BINDING 300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT BINDING 302
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 331
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
SQ SEQUENCE 371 AA; 41220 MW; AE01BA91CCD0CB40 CRC64;
MSYELLATDG KARRGRLTFP RGEVETPAFM PVGTYGTVKG MLPRDIEEIG AHMILGNTFH
LMLRPGTEVV KAHGDLHDFV QWKGPILTDS GGFQVFSLGD MRKITEAGVN FQSPVDGSPV
TLNPEISMQV QKDLGSDVVM IFDECTPYPA TETQSAESMR LSLRWAKRSK EAHGDSPAAL
FGIVQGGMFP ELRDESLAGL TEIGFDGYAI GGLSVGEPKD EMMKILDHTT PKMPEDRPRY
LMGVGRPEDL VEGVKRGVDM FDCVMPTRNA RNGHLFVSTG VVKIRNAAHK HDDGPLDREC
DCYTCKNFSR AYLHHLDKCK EMLGAQLNTI HNLRHYQNLM SGLRTAIEQG RLGDFVEEFY
KKRGQETPAL D
//
