ID   TGT_AERHH               Reviewed;         378 AA.
AC   A0KJ20;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   16-JUN-2009, entry version 16.
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=AHA_1735;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / NCIB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(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; CP000462; ABK37967.1; -; Genomic_DNA.
DR   RefSeq; YP_856271.1; -.
DR   GeneID; 4490304; -.
DR   GenomeReviews; CP000462_GR; AHA_1735.
DR   KEGG; aha:AHA_1735; -.
DR   TIGR; AHA_1735; -.
DR   OMA; A0KJ20; 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    378       Queuine tRNA-ribosyltransferase.
FT                                /FTId=PRO_1000016760.
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   378 AA;  43001 MW;  7E8AC59F6BA129B4 CRC64;
     MKFELKTTDG RARRGQLVFE RGTVQTPAFM PVGTYGTVKG MTPEEVRETG AQILLGNTFH
     LWLRPGQEVM RAHGDLHDFM NWQGPILTDS GGFQVFSLGH IRKITEAGVH FRHPINGEKI
     FLDPEKSMEI QYDLGSDIVM IFDECTPYPA TYEEARKSME MSLRWGKRSR DKFDALGNKN
     ALFGIIQGSV YEDLRDVSLD GLLEIGFDGY AVGGLAVGEP KEDMHRILEH VCPKIPADKP
     RYLMGVGKPE DLVEGVRRGI DMFDCVMPTR NARNGHLFTT DGVVKIRNAK YREDTSTLDA
     DCDCYTCKNY TRSYLYHLDK CNEILGARLN TIHNLRYYQR VMQGLRDAIE QGKLDDFVTE
     FYRRQGKPVP PLAENDVK
//