ID   TGT_BORBU               Reviewed;         375 AA.
AC   O51749;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   16-JUN-2009, entry version 60.
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=BB_0809;
OS   Borrelia burgdorferi (Lyme disease spirochete).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia;
OC   Borrelia burgdorferi group.
OX   NCBI_TaxID=139;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / B31 / CIP 102532 / DSM 4680;
RX   MEDLINE=98065943; PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K.,
RA   Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D.,
RA   Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J.,
RA   Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D.,
RA   Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A.,
RA   Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K.,
RA   Roberts K.M., Hatch B., Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia
RT   burgdorferi.";
RL   Nature 390:580-586(1997).
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; AE000783; AAC67147.1; -; Genomic_DNA.
DR   PIR; H70200; H70200.
DR   RefSeq; NP_212943.1; -.
DR   HSSP; P28720; 1K4G.
DR   GeneID; 1195667; -.
DR   GenomeReviews; AE000783_GR; BB_0809.
DR   KEGG; bbu:BB0809; -.
DR   NMPDR; fig|224326.1.peg.1193; -.
DR   TIGR; BB_0809; -.
DR   HOGENOM; O51749; -.
DR   OMA; O51749; ECVRLPA.
DR   BioCyc; BBUR224326:BB_0809-MON; -.
DR   BRENDA; 2.4.2.29; 142596.
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_0000135453.
FT   ACT_SITE     90     90       Nucleophile (By similarity).
FT   METAL       305    305       Zinc (By similarity).
FT   METAL       307    307       Zinc (By similarity).
FT   METAL       310    310       Zinc (By similarity).
FT   METAL       336    336       Zinc (By similarity).
FT   BINDING      91     91       Substrate (By similarity).
SQ   SEQUENCE   375 AA;  43199 MW;  7D7A554644439763 CRC64;
     MFSVIKNDKH FNARVGFLNL PHGRVDIPCF MPVGTLGAMK GLKHAVLEKL ECNLMLANTY
     HLYLRLGIKT VEKYVGLHNF TIWNKNFLTD SGGFRVFSFS DLRKIDLKGV HFKSHIDGSY
     HYFTSEGIFA MQEIFGSDII MPLDICSSYG IDYNEANLYT NITTNWASST FKSSKNRKEG
     YNGLLFLITQ GNFFKDLRKR SINDILELDS PGIAIGGISV GEPREKYLEI LEYSFLLIPK
     EKPRYVMGIG TPHYILNAIY YGIDIFDCFN PARITRHGSL LTDNGIMCIG RKEYKDDTSK
     VEKNCICTLC KRYSRGYLRH LIKSKELFGI VLASEHNIHY MFRLISKIRA AILNDDFLNF
     RTSYLKKYEE ENFDE
//