ID A0A1X0URW7_9NOCA Unreviewed; 423 AA.
AC A0A1X0URW7;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=BJI47_09265 {ECO:0000313|EMBL:ORI24334.1};
OS Rhodococcus sp. 1168.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=2018041 {ECO:0000313|EMBL:ORI24334.1, ECO:0000313|Proteomes:UP000192546};
RN [1] {ECO:0000313|EMBL:ORI24334.1, ECO:0000313|Proteomes:UP000192546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1168 {ECO:0000313|EMBL:ORI24334.1,
RC ECO:0000313|Proteomes:UP000192546};
RA Nahar A.;
RT "Metabolic and lipid synthesis pathways analysis of sub-Antarctic
RT Rhodococcus luteus.";
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 -!- 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:ORI24334.1}.
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DR EMBL; MKKY01000035; ORI24334.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X0URW7; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000192546; 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:UP000192546};
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 30..415
FT /note="tRNA-guanine(15) transglycosylase-like"
FT /evidence="ECO:0000259|Pfam:PF01702"
FT ACT_SITE 107
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT ACT_SITE 316
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT BINDING 107..111
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT BINDING 269
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT BINDING 354
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT BINDING 356
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT BINDING 359
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT BINDING 385
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
SQ SEQUENCE 423 AA; 47098 MW; 638526938ADF300B CRC64;
MRRSSPKVGR VSAPNDPYFD IDSRLDGQLG RTGTIHTPHG DIATPAFIAV GTKATVKAVL
PEAMKELGAQ AVLANAYHLY LQPGSDIIDE AGGLGKFMNW DGPTFTDSGG FQVMSLGVGF
KKVISMDASR VESDDVIAEG KERLAHVDDD GVTFKSHLDG SKHRFTPEVS MQIQHRLGAD
IMFAFDELTT LMNTRGYQEL SVDRTQAWAV RCVEEHERLT AERVGKPYQA LFGVVQGAQY
EDLRRKAAHD LETITGETGR GFDGYGIGGA LEKQNLGTIV RWVNEELPEH KPRHMLGISE
PDDFFTAIEN GADTFDCVNP SRVARNAAIY VPTGRFNINT AKNRRDFTPI DEHCDCYTCA
HYTRAYIHHL FKAKEMLAST LCTIHNERFT VKLVDDIRAS INEGRFEELK TEYLGRFYGT
VSR
//
