ID   D2NPM3_ROTMD            Unreviewed;       466 AA.
AC   D2NPM3;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   02-DEC-2020, entry version 74.
DE   RecName: Full=Queuine tRNA-ribosyltransferase {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777};
DE            EC=2.4.2.29 {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777};
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   OrderedLocusNames=RMDY18_17590 {ECO:0000313|EMBL:BAI65591.1};
OS   Rothia mucilaginosa (strain DY-18) (Stomatococcus mucilaginosus).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Rothia.
OX   NCBI_TaxID=680646 {ECO:0000313|EMBL:BAI65591.1, ECO:0000313|Proteomes:UP000001883};
RN   [1] {ECO:0000313|Proteomes:UP000001883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY-18 {ECO:0000313|Proteomes:UP000001883};
RA   Yamane K., Nambu T., Mashimo C., Sugimori C., Yamanaka T., Leung K.,
RA   Fukushima H.;
RT   "Complete genome sequence of Rothia mucilaginosa DJ.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAI65591.1, ECO:0000313|Proteomes:UP000001883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY-18 {ECO:0000313|EMBL:BAI65591.1,
RC   ECO:0000313|Proteomes:UP000001883};
RA   Yamane K., Yoshida M., Fujihira T., Baba T., Tsuji N., Hayashi H.,
RA   Sugimori C., Yamanaka T., Mashimo C., Nambu T., Kawai H., Fukushima H.;
RT   "Isolation and identification of Rothia mucilaginosa from persistent apical
RT   periodontitis lesions.";
RL   J Osaka Dent Univ 44:93-98(2010).
RN   [3] {ECO:0000313|EMBL:BAI65591.1, ECO:0000313|Proteomes:UP000001883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY-18 {ECO:0000313|EMBL:BAI65591.1,
RC   ECO:0000313|Proteomes:UP000001883};
RA   Yamane K., Nambu T., Yamanaka T., Mashimo C., Sugimori C., Leung K.-P.,
RA   Fukushima H.;
RT   "Complete Genome Sequence of Rothia mucilaginosa DY-18: A Clinical Isolate
RT   with Dense Meshwork-Like Structures from a Persistent Apical Periodontitis
RT   Lesion.";
RL   Sequencing 2010:457236-457236(2010).
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       ECO:0000256|RuleBase:RU003777}.
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, ECO:0000256|RuleBase:RU003777};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00168,
CC         ECO:0000256|RuleBase:RU003777};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00168,
CC       ECO:0000256|RuleBase:RU003777};
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, ECO:0000256|RuleBase:RU003777}.
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; AP011540; BAI65591.1; -; Genomic_DNA.
DR   STRING; 680646.RMDY18_17590; -.
DR   EnsemblBacteria; BAI65591; BAI65591; RMDY18_17590.
DR   KEGG; rmu:RMDY18_17590; -.
DR   eggNOG; COG0343; Bacteria.
DR   HOGENOM; CLU_022060_0_0_11; -.
DR   OMA; GIDLFDC; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000001883; 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   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 {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW   Rule:MF_00168, ECO:0000256|RuleBase:RU003777};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00168};
KW   Queuosine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00168};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001883};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00168, ECO:0000256|RuleBase:RU003777, ECO:0000313|EMBL:BAI65591.1};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_00168, ECO:0000256|RuleBase:RU003777};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777}.
FT   DOMAIN          71..461
FT                   /note="TGT"
FT                   /evidence="ECO:0000259|Pfam:PF01702"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          148..152
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   REGION          364..368
FT                   /note="RNA binding; important for wobble base 34
FT                   recognition"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   ACT_SITE        148
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   ACT_SITE        359
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   METAL           397
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   METAL           399
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   METAL           402
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   METAL           428
FT                   /note="Zinc; via pros nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   BINDING         235
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   BINDING         285
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   BINDING         312
FT                   /note="Substrate; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
SQ   SEQUENCE   466 AA;  51371 MW;  D80AECC5B94CCDA7 CRC64;
     MRTPPPAKEA GFSGRLGCRH SDGKQTIERR MSVLDNSFPT EDFGFTITSR LADTASPSAE
     RVEANGGQFR GRTGVITTPH GQIQTPAFTP VGTKATVKAV LPESMKELGA QALLSNAYHL
     YLQPGPEILD AAGGLGAFMN WDGPTFTDSG GFQVMSLGSG FKKVIDMGTV ADAKGADGRP
     LGDDDVAKGK ERLAHIDDDG VNFKSHIDGS IHRFTPEVSM QVQHQIGADV MFAFDELTTL
     YNSRGYQEEA LERTRLWALR CIAEHQRLTA ERVGKPYQAL FGVIQGAQYE DLRRKACQDL
     GSMPFDGFGI GGALEKENLG TIVRWCAEEL PESKPRHLLG ISEPDDIFVG IENGVDTFDC
     VSPTRVARNA AVYSPTGRYN ITNARFKADF SPIYEGCDCY TCTHYTRAYL RHLFKADERL
     AATLASIHNE RFIVRMVDDA REAIKDGTYF EYRDEFLGNY YSGKKP
//