ID   TGT_CAMJR               Reviewed;         373 AA.
AC   Q5HUF2;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   16-JUN-2009, entry version 27.
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=CJE1090;
OS   Campylobacter jejuni (strain RM1221).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=195099;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15660156; DOI=10.1371/journal.pbio.0030015;
RA   Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A.,
RA   Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C.,
RA   Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U.,
RA   Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M.,
RA   Nelson K.E.;
RT   "Major structural differences and novel potential virulence mechanisms
RT   from the genomes of multiple Campylobacter species.";
RL   PLoS Biol. 3:72-85(2005).
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; CP000025; AAW35418.1; -; Genomic_DNA.
DR   RefSeq; YP_179083.1; -.
DR   GeneID; 3231599; -.
DR   GenomeReviews; CP000025_GR; CJE1090.
DR   KEGG; cjr:CJE1090; -.
DR   NMPDR; fig|195099.3.peg.1171; -.
DR   TIGR; CJE1090; -.
DR   HOGENOM; Q5HUF2; -.
DR   OMA; Q5HUF2; ECVRLPA.
DR   BioCyc; CJEJ195099:CJE_1090-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    373       Queuine tRNA-ribosyltransferase.
FT                                /FTId=PRO_0000135460.
FT   ACT_SITE     90     90       Nucleophile (By similarity).
FT   METAL       308    308       Zinc (By similarity).
FT   METAL       310    310       Zinc (By similarity).
FT   METAL       313    313       Zinc (By similarity).
FT   METAL       339    339       Zinc (By similarity).
FT   BINDING      91     91       Substrate (By similarity).
SQ   SEQUENCE   373 AA;  42554 MW;  23197D2141F32B18 CRC64;
     MEFKLKHKDG MARVCEITTA HSTFLTPVFM PVGTVGAVKS LDANDMKNEL DAKIILANTY
     HMYLRPTSKV VKDFGGLHGF TKFDRSFLTD SGGFQAFSLS KNSKHFNEGI EFKSHIDGSR
     HLFTPKSVLD AQYDFNSDIM MILDDLVALP ATKERVKISV DRTILWAKEA ITYHKNMQNK
     GIGIGQNIFG IIQGGTDYEE RKRCALSLNE MPFDGLAIGG LSVGEENALM YETVQNLNPY
     LDENRPRYLM GVGTPEDLVE NVERGVDMFD CVMPTRNARN GTFFTSFGKF NIKKAEFIND
     HEVIDPTCSC YTCRNFSRGY LNHLFKAKEL TFFRLASLHN LHYYLELARK MREAILNNSF
     TQFKRNFYHL RGK
//