ID   TGT_BACHD               Reviewed;         379 AA.
AC   Q9KDI5;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   16-JUN-2009, entry version 46.
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=BH1228;
OS   Bacillus halodurans.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=86665;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / C-125 / DSM 18197 / FERM 7344 / JCM 9153;
RX   MEDLINE=20512582; PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N.,
RA   Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S.,
RA   Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus
RT   halodurans and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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; BA000004; BAB04947.1; -; Genomic_DNA.
DR   PIR; D83803; D83803.
DR   RefSeq; NP_242094.1; -.
DR   HSSP; P28720; 1K4G.
DR   GeneID; 894208; -.
DR   GenomeReviews; BA000004_GR; BH1228.
DR   KEGG; bha:BH1228; -.
DR   NMPDR; fig|272558.1.peg.1228; -.
DR   HOGENOM; Q9KDI5; -.
DR   OMA; Q9KDI5; VLNSDIV.
DR   BioCyc; BHAL272558:BH1228-MON; -.
DR   BRENDA; 2.4.2.29; 191865.
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    379       Queuine tRNA-ribosyltransferase.
FT                                /FTId=PRO_0000135448.
FT   ACT_SITE     94     94       Nucleophile (By similarity).
FT   METAL       306    306       Zinc (By similarity).
FT   METAL       308    308       Zinc (By similarity).
FT   METAL       311    311       Zinc (By similarity).
FT   METAL       337    337       Zinc (By similarity).
FT   BINDING      95     95       Substrate (By similarity).
SQ   SEQUENCE   379 AA;  43062 MW;  E40D187CE6BAE380 CRC64;
     MAAVTYELIK TCKQSGARLG KLHTPHGTIE TPIFMPVGTL ATVKTMSPEE LKQLGAQIIL
     SNTYHLWLRP GHDIVKEAGG LHEFMNWDRP ILTDSGGFQV FSLSDLRTIE EEGVHFRNHL
     SGEKLFLSPE GAMEIQNALG SDIMMAFDEC PPYPAERDYM RPSVERTSRW AERCLKAHKR
     PEDQALFGII QGGEYEDLRR QSAQDITSLD FPGYAIGGVS VGEPKDVMNR VLEFTTPLLP
     ANKPRYLMGV GSPDSLIDGA IRGIDMFDCV LPTRIARNGT CMTSNGRLVV RNAKYARDFR
     SLDENCDCHV CQTYTRAYIR HLVKCDETFG FRLTTYHNLY FLLKLMKDVR QAILDDRLLD
     FREEFFEQYG FNQPNAKNF
//