ID   D2NPM3_ROTMD            Unreviewed;       466 AA.
AC   D2NPM3;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   16-MAR-2016, entry version 48.
DE   RecName: Full=Queuine tRNA-ribosyltransferase {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00087750};
DE            EC=2.4.2.29 {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00087822};
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|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.
CC   -!- FUNCTION: Exchanges the guanine residue with 7-aminomethyl-7-
CC       deazaguanine in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His
CC       and -Tyr). After this exchange, a cyclopentendiol moiety is
CC       attached to the 7-aminomethyl group of 7-deazaguanine, resulting
CC       in the hypermodified nucleoside queuosine (Q) (7-(((4,5-cis-
CC       dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
CC       {ECO:0000256|HAMAP-Rule:MF_00168}.
CC   -!- FUNCTION: Exchanges the guanine residue with 7-aminomethyl-7-
CC       deazaguanine in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His
CC       and -Tyr). After this exchange, a cyclopentendiol moiety is
CC       attached to the 7-aminomethyl group of 7-deazaguanine, resulting
CC       in the hypermodified nucleoside queuosine (Q) (7-(((4,5-cis-
CC       dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine) (By
CC       similarity). {ECO:0000256|SAAS:SAAS00206996}.
CC   -!- CATALYTIC ACTIVITY: Guanine(34) in tRNA + 7-aminomethyl-7-
CC       carbaguanine = 7-aminomethyl-7-carbaguanine(34) in tRNA + guanine.
CC       {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777,
CC       ECO:0000256|SAAS:SAAS00087626}.
CC   -!- CATALYTIC ACTIVITY: Guanine(34) in tRNA + queuine = queuosine(34)
CC       in tRNA + guanine. {ECO:0000256|HAMAP-Rule:MF_00168,
CC       ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00087703}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00168, ECO:0000256|RuleBase:RU003777};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00168, ECO:0000256|RuleBase:RU003777};
CC   -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|SAAS:SAAS00087869}.
CC   -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777}.
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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   PATRIC; 35273999; VBIRotMuc152186_1520.
DR   eggNOG; ENOG4105C6U; Bacteria.
DR   eggNOG; COG0343; LUCA.
DR   HOGENOM; HOG000223473; -.
DR   KO; K00773; -.
DR   OMA; TPRFMPV; -.
DR   OrthoDB; EOG6SNDVG; -.
DR   BioCyc; RMUC680646:GH63-1734-MONOMER; -.
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-HAMAP.
DR   GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR   Gene3D; 3.20.20.105; -; 2.
DR   HAMAP; MF_00168; Q_tRNA_Tgt; 1.
DR   InterPro; IPR004803; Queuine_tRNA-ribosylTrfase.
DR   InterPro; IPR002616; tRNA_ribo_trans-like.
DR   Pfam; PF01702; TGT; 1.
DR   SUPFAM; SSF51713; SSF51713; 2.
DR   TIGRFAMs; TIGR00430; Q_tRNA_tgt; 1.
DR   TIGRFAMs; TIGR00449; tgt_general; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001883};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00168,
KW   ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00468650};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00168,
KW   ECO:0000256|SAAS:SAAS00460860};
KW   Queuosine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00168,
KW   ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00460855};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001883};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00168,
KW   ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00468820,
KW   ECO:0000313|EMBL:BAI65591.1};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00168,
KW   ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00460804};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777,
KW   ECO:0000256|SAAS:SAAS00460797}.
FT   ACT_SITE    148    148       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_00168}.
FT   METAL       397    397       Zinc. {ECO:0000256|HAMAP-Rule:MF_00168}.
FT   METAL       399    399       Zinc. {ECO:0000256|HAMAP-Rule:MF_00168}.
FT   METAL       402    402       Zinc. {ECO:0000256|HAMAP-Rule:MF_00168}.
FT   METAL       428    428       Zinc. {ECO:0000256|HAMAP-Rule:MF_00168}.
FT   BINDING     149    149       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                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
//