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TGT_CLOP1
ID   TGT_CLOP1               Reviewed;         380 AA.
AC   Q0TP15;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Queuine tRNA-ribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00168};
DE            EC=2.4.2.29 {ECO:0000255|HAMAP-Rule:MF_00168};
DE   AltName: Full=Guanine insertion enzyme {ECO:0000255|HAMAP-Rule:MF_00168};
DE   AltName: Full=tRNA-guanine transglycosylase {ECO:0000255|HAMAP-Rule:MF_00168};
GN   Name=tgt {ECO:0000255|HAMAP-Rule:MF_00168}; OrderedLocusNames=CPF_2201;
OS   Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB
OS   6125 / NCTC 8237 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC   Type A;
RX   PubMed=16825665; DOI=10.1101/gr.5238106;
RA   Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA   Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA   Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA   Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA   Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA   Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA   Paulsen I.T.;
RT   "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT   Clostridium perfringens.";
RL   Genome Res. 16:1031-1040(2006).
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:0000255|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:0000255|HAMAP-
CC         Rule:MF_00168};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00168};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00168};
CC   -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC       {ECO:0000255|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:0000255|HAMAP-Rule:MF_00168}.
CC   -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00168}.
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DR   EMBL; CP000246; ABG82825.1; -; Genomic_DNA.
DR   RefSeq; WP_003451459.1; NC_008261.1.
DR   AlphaFoldDB; Q0TP15; -.
DR   SMR; Q0TP15; -.
DR   STRING; 195103.CPF_2201; -.
DR   EnsemblBacteria; ABG82825; ABG82825; CPF_2201.
DR   GeneID; 29570693; -.
DR   KEGG; cpf:CPF_2201; -.
DR   eggNOG; COG0343; Bacteria.
DR   HOGENOM; CLU_022060_0_1_9; -.
DR   OMA; GIDLFDC; -.
DR   OrthoDB; 1165356at2; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000001823; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008479; F:queuine tRNA-ribosyltransferase 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; -; 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   Pfam; PF01702; TGT; 1.
DR   SUPFAM; SSF51713; SSF51713; 1.
DR   TIGRFAMs; TIGR00430; Q_tRNA_tgt; 1.
DR   TIGRFAMs; TIGR00449; tgt_general; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Metal-binding; Queuosine biosynthesis; Transferase;
KW   tRNA processing; Zinc.
FT   CHAIN           1..380
FT                   /note="Queuine tRNA-ribosyltransferase"
FT                   /id="PRO_1000016782"
FT   REGION          256..262
FT                   /note="RNA binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT   REGION          280..284
FT                   /note="RNA binding; important for wobble base 34
FT                   recognition"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT   ACT_SITE        93
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT   ACT_SITE        275
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT   BINDING         93..97
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT   BINDING         147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT   BINDING         198
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT   BINDING         225
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT   BINDING         313
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT   BINDING         315
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT   BINDING         318
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT   BINDING         344
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
SQ   SEQUENCE   380 AA;  43186 MW;  113B6B73540539D6 CRC64;
     MTKKRYTLLK KDGKARRGEF VTPHGTIQTP VFMNVGTLAA IKGAVSSMDL KEIGCQVELS
     NTYHLHLRPG DKIVKQMGGL HNFMNWDRPI LTDSGGFQVF SLAGMRKIKE EGVYFNSHID
     GRKIFMGPEE SMQIQSNLGS TIAMAFDECI PNPSTREYVE KSVARTTRWL ERCKKEMDRL
     NSLDDTVNKE QMLFGINQGG VYEDIRIEHA KTIREMDLDG YAIGGLAVGE THEEMYRVID
     AVVPHLPEDK PIYLMGVGLP SNILEAVERG VDFFDCVLPA RNGRHGHVFT KEGKINLMNA
     KFELDARPID EGCQCPACKN YTRAYIRHLF KAKEMLAMRL CVLHNLYFYN KLMEDIRDAI
     DGGYFAEFKA KKLEEWNGRA
 
 
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