ID   D2NPM3_ROTMD            Unreviewed;       466 AA.
AC   D2NPM3;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   28-FEB-2018, entry version 62.
DE   RecName: Full=Queuine tRNA-ribosyltransferase {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|SAAS:SAAS00102053};
DE            EC=2.4.2.29 {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|SAAS:SAAS00384033};
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.
CC   -!- FUNCTION: Catalyzes the base-exchange of a guanine (G) residue
CC       with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at
CC       position 34 (anticodon wobble position) in tRNAs with GU(N)
CC       anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs
CC       through a double-displacement mechanism. The nucleophile active
CC       site attacks the C1' of nucleotide 34 to detach the guanine base
CC       from the RNA, forming a covalent enzyme-RNA intermediate. The
CC       proton acceptor active site deprotonates the incoming PreQ1,
CC       allowing a nucleophilic attack on the C1' of the ribose to form
CC       the product. After dissociation, two additional enzymatic
CC       reactions on the tRNA convert PreQ1 to queuine (Q), resulting in
CC       the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-
CC       cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
CC       {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|SAAS:SAAS00628203}.
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|SAAS:SAAS00102009}.
CC   -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|SAAS:SAAS00384008}.
CC   -!- SUBUNIT: Homodimer. Within each dimer, one monomer is responsible
CC       for RNA recognition and catalysis, while the other monomer binds
CC       to the replacement base PreQ1. {ECO:0000256|SAAS:SAAS00628204}.
CC   -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|SAAS:SAAS01002254}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of 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; ENOG4105C6U; Bacteria.
DR   eggNOG; COG0343; LUCA.
DR   HOGENOM; HOG000223473; -.
DR   KO; K00773; -.
DR   OMA; TYHLFLR; -.
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; 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|SAAS:SAAS01002259};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00168,
KW   ECO:0000256|SAAS:SAAS00087792};
KW   Queuosine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00168,
KW   ECO:0000256|SAAS:SAAS00087839};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001883};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00168,
KW   ECO:0000256|SAAS:SAAS00876991, ECO:0000313|EMBL:BAI65591.1};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00168,
KW   ECO:0000256|SAAS:SAAS00087682};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|SAAS:SAAS00460797}.
FT   DOMAIN      219    456       TGT. {ECO:0000259|Pfam:PF01702}.
FT   REGION      148    152       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00168}.
FT   REGION      364    368       RNA binding; important for wobble base 34
FT                                recognition. {ECO:0000256|HAMAP-Rule:
FT                                MF_00168}.
FT   ACT_SITE    148    148       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00168}.
FT   ACT_SITE    359    359       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; via pros nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00168}.
FT   BINDING     235    235       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00168}.
FT   BINDING     285    285       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00168}.
FT   BINDING     312    312       Substrate; via amide nitrogen.
FT                                {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
//