ID   TGT_BACHK               Reviewed;         379 AA.
AC   Q6HDA9;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 31.
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=BT9727_4150;
OS   Bacillus thuringiensis subsp. konkukian.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=180856;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=97-27;
RX   PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S.,
RA   Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O.,
RA   Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T.,
RA   Goodwin L.A., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA   Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K.,
RA   Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C.,
RA   Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P.,
RA   Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G.,
RA   Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA   Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(2006).
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; AE017355; AAT63704.1; -; Genomic_DNA.
DR   RefSeq; YP_038467.1; -.
DR   GeneID; 2855578; -.
DR   GenomeReviews; AE017355_GR; BT9727_4150.
DR   KEGG; btk:BT9727_4150; -.
DR   HOGENOM; Q6HDA9; -.
DR   OMA; Q6HDA9; MAFDQCP.
DR   BioCyc; BTHU281309:BT9727_4150-MON; -.
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_0000135449.
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;  43227 MW;  6DE1E29B88568644 CRC64;
     MTAIRYEFIK TCKQTGARLG RVHTPHGSFD TPTFMPVGTL ATVKTMSPEE LKAMDSGIIL
     SNTYHLWLRP GHEIIREAGG LHKFMNWDRA ILTDSGGFQV FSLSDFRRIE EEGVHFRNHL
     NGDKLFLSPE KAMEIQNALG SDIMMAFDEC PPFPATFEYM KKSVERTSRW AERCLKAHER
     PQDQGLFGIV QGGEFEELRR QSAKDLVSMD FPGYAVGGLS VGEPKDIMNR VLEFTTPLLP
     DNKPRYLMGV GSPDSLIDGA IRGIDMFDCV LPTRIARNGT CMTSEGRLVV KNAKFARDFG
     PLDPNCDCYT CKNYSRAYIR HLMKCDETFG IRLTSYHNLH FLLNLMEQVR QAIREDRLGD
     FREEFFEQYG FNKPNAKNF
//