ID   TGT_ECOK1               Reviewed;         375 AA.
AC   A1A876;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   16-JUN-2009, entry version 17.
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=Ecok1_03720; ORFNames=APECO1_1604;
OS   Escherichia coli O1:K1 / APEC.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17293413; DOI=10.1128/JB.01726-06;
RA   Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P.,
RA   Johnson S.J., Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R.,
RA   Nolan L.K.;
RT   "The genome sequence of avian pathogenic Escherichia coli strain
RT   O1:K1:H7 shares strong similarities with human extraintestinal
RT   pathogenic E. coli genomes.";
RL   J. Bacteriol. 189:3228-3236(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; CP000468; ABI99865.1; -; Genomic_DNA.
DR   RefSeq; YP_851580.1; -.
DR   GeneID; 4492479; -.
DR   GenomeReviews; CP000468_GR; Ecok1_03720.
DR   KEGG; ecv:APECO1_1604; -.
DR   OMA; A1A876; VLNSDIV.
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    375       Queuine tRNA-ribosyltransferase.
FT                                /FTId=PRO_1000016787.
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       333    333       Zinc (By similarity).
FT   BINDING      90     90       Substrate (By similarity).
SQ   SEQUENCE   375 AA;  42594 MW;  40271CA08D8A8820 CRC64;
     MKFELDTTDG RARRGRLVFD RGVVETPCFM PVGTYGTVKG MTPEEVEATG AQIILGNTFH
     LWLRPGQEIM KLHGDLHDFM QWKGPILTDS GGFQVFSLGD IRKITEQGVH FRNPINGDPI
     FLDPEKSMEI QYDLGSDIVM IFDECTPYPA DWDYAKRSME MSLRWAKRSR ERFDSLGNKN
     ALFGIIQGSV YEDLRDISVK GLVDIGFDGY AVGGLAVGEP KADMHRILEH VCPQIPADKP
     RYLMGVGKPE DLVEGVRRGI DMFDCVMPTR NARNGHLFVT DGVVKIRNAK YKSDTGPLDP
     ECDCYTCRNY SRAYLHHLDR CNEILGARLN TIHNLRYYQR LMAGLRKAIE EGKLESFVTD
     FYQRQGREVP PLNVD
//