ID   TGT_BACA2               Reviewed;         381 AA.
AC   A7Z766;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   16-JUN-2009, entry version 11.
DE   RecName: Full=Queuine tRNA-ribosyltransferase;
DE            EC=2.4.2.29;
DE   AltName: Full=tRNA-guanine transglycosylase;
DE   AltName: Full=Guanine insertion enzyme;
GN   Name=tgt; OrderedLocusNames=RBAM_024820;
OS   Bacillus amyloliquefaciens (strain FZB42).
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=326423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17704766; DOI=10.1038/nbt1325;
RA   Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA   Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA   Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA   Strittmatter A., Gottschalk G., Borriss R.;
RT   "Comparative analysis of the complete genome sequence of the plant
RT   growth-promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL   Nat. Biotechnol. 25:1007-1014(2007).
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).
CC   -!- CATALYTIC ACTIVITY: [tRNA]-guanine + queuine = [tRNA]-queuine +
CC       guanine.
CC   -!- CATALYTIC ACTIVITY: [tRNA]-guanine + 7-aminomethyl-7-carbaguanine
CC       = [tRNA]-7-aminomethyl-7-carbaguanine + guanine.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- PATHWAY: tRNA modification; queuosine-tRNA biosynthesis.
CC   -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.
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DR   EMBL; CP000560; ABS74842.1; -; Genomic_DNA.
DR   RefSeq; YP_001422073.1; -.
DR   GeneID; 5462891; -.
DR   GenomeReviews; CP000560_GR; RBAM_024820.
DR   KEGG; bay:RBAM_024820; -.
DR   OMA; A7Z766; MAFDQCP.
DR   GO; GO:0008479; F:queuine tRNA-ribosyltransferase activity; IEA:HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008616; P:queuosine biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00168; -; 1.
DR   InterPro; IPR004803; QtRNA_ribo_trans.
DR   InterPro; IPR002616; tRNA_ribo_trans.
DR   Gene3D; G3DSA:3.20.20.105; tRNA_ribo_trans; 1.
DR   PANTHER; PTHR11962; tRNA_ribo_trans; 1.
DR   Pfam; PF01702; TGT; 1.
DR   TIGRFAMs; TIGR00430; Q_tRNA_tgt; 1.
DR   TIGRFAMs; TIGR00449; tgt_general; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Glycosyltransferase; Metal-binding;
KW   Queuosine biosynthesis; Transferase; tRNA processing; Zinc.
FT   CHAIN         1    381       Queuine tRNA-ribosyltransferase.
FT                                /FTId=PRO_1000016763.
FT   ACT_SITE     96     96       Nucleophile (By similarity).
FT   METAL       308    308       Zinc (By similarity).
FT   METAL       310    310       Zinc (By similarity).
FT   METAL       313    313       Zinc (By similarity).
FT   METAL       339    339       Zinc (By similarity).
FT   BINDING      97     97       Substrate (By similarity).
SQ   SEQUENCE   381 AA;  43666 MW;  01E35AD4B9C5DFAB CRC64;
     MAEQPIRYEF IKECKQTGAR LGRVHTPHGS FETPVFMPVG TLATVKTMSP DELKSMDAGI
     ILSNTYHLWL RPGHDIVKEA GGLHKFMNWD RAILTDSGGF QVFSLSKFRN IEEEGVHFRN
     HLNGDKLFLS PEKAMEIQNA LGSDIMMAFD ECPPYPAEYD YMKRSVERTS RWAERCLEAH
     GRSDEQGLFG IVQGGEYEDL RTQSAKDLVS LDFPGYAIGG LSVGEPKHVM NRVLEFTTPL
     LPKDKPRYLM GVGSPDALID GAIRGVDMFD CVLPTRIARN GTVFTNEGRL NMKNAKYERD
     FRPIDEECSC HTCKNYSRAY IRHLIRCNET FGIRLTTYHN LHFLLHLMEQ VRQAIREDRL
     GDFREEFFER YGYNKPNAKS F
//