ID   TGT_BLOFL               Reviewed;         378 AA.
AC   Q7VQB1;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   16-JUN-2009, entry version 33.
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=Bfl230;
OS   Blochmannia floridanus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=203907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22784745; PubMed=12886019; DOI=10.1073/pnas.1533499100;
RA   Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F.,
RA   Latorre A., Rausell C., Kamerbeek J., Gadau J., Hoelldobler B.,
RA   van Ham R.C.H.J., Gross R., Moya A.;
RT   "The genome sequence of Blochmannia floridanus: comparative analysis
RT   of reduced genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003).
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; BX248583; CAD83743.1; -; Genomic_DNA.
DR   RefSeq; NP_878527.1; -.
DR   HSSP; P28720; 1PXG.
DR   GeneID; 1499430; -.
DR   GenomeReviews; BX248583_GR; Bfl230.
DR   KEGG; bfl:Bfl230; -.
DR   HOGENOM; Q7VQB1; -.
DR   OMA; Q7VQB1; VLNSDIV.
DR   BioCyc; CBLO203907:BFL230-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    378       Queuine tRNA-ribosyltransferase.
FT                                /FTId=PRO_0000135461.
FT   ACT_SITE     89     89       Nucleophile (By similarity).
FT   METAL       302    302       Zinc (By similarity).
FT   METAL       304    304       Zinc (By similarity).
FT   METAL       307    307       Zinc (By similarity).
FT   METAL       334    334       Zinc (By similarity).
FT   BINDING      90     90       Substrate (By similarity).
SQ   SEQUENCE   378 AA;  43608 MW;  99C8ECE4ADAAACDD CRC64;
     MVFRVLQTDG DARVGKLTCH HGIIETPAFI PVGTYGVVKS VTSQEVAESG AQIILSNTFH
     LWLRPGLEII KIHQNLHKFM NWMGPIITDS GGFQVFSLNK LRKITESGVY FKDPVNGSTI
     FLTPEKSMDI QYHLGSDIVL VFDECVSYPS TWEYIKNSVE ISLNWAERSR LHFDKLHNSN
     MLFAIIQGGM YEELRNRSAQ ELINIKFDGY AIGGLSVGET PQERFRIVSY VCKIIPFDKP
     RYLMGVGKPQ DLIEAVCLGV DMFDCVIPTR NARNGYLFTN NGVVRIRNAK YESDLDPIEE
     DCDCYTCQRY YSRSYLHYLD RCNESLGIRL NTIHNLRYYQ RLMEEIRQSI RMKKLRKFVE
     AFNYKFNSVS TNNYLSNI
//