ID TGT_CAMFF Reviewed; 374 AA. AC A0RPL5; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, 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=CFF8240_0980; OS Campylobacter fetus subsp. fetus (strain 82-40). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=360106; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Fouts D.E., Nelson K.E.; RT "Sequence of Campylobacter fetus subsp. fetus 82-40."; RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases. 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000487; ABK81825.1; -; Genomic_DNA. DR RefSeq; YP_892148.1; -. DR GeneID; 4537752; -. DR GenomeReviews; CP000487_GR; CFF8240_0980. DR KEGG; cff:CFF8240_0980; -. DR NMPDR; fig|360106.5.peg.934; -. DR TIGR; CFF8240_0980; -. DR OMA; A0RPL5; ECVRLPA. 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 1 374 Queuine tRNA-ribosyltransferase. FT /FTId=PRO_1000016769. 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 374 AA; 42297 MW; 0A48196FCBAEE4EB CRC64; MNFKIDKTDG NARACTLQTA HSTIQTPIFM PVGTLGAVKS LDAIDLKEIL DAKIILANTY HLYLRPTSKV VREFGGLHGF SKFDRSFLTD SGGFQAFSLS KISKPDENGI KFKSHIDGSM HYFTPKSVLD TQYDLSSDIM MILDDLVALP ATKERIDLSI KRTINWAKIA CEYHKSNKQK SVGIDQNIFG IIQGGTDYNA RKLCAEALCE MEFDGLAIGG LSVGESNEEM YDTVEALMPF IDKNRPRYLM GVGTPEDLVQ NVERGVDMFD CVMPTRNARN GTLFTSFGKI NIKSAAFIKD DNKIDPECDC YTCSNFSRGY LNHLYKAREL TFFRLASLHN LHYYLNLVKQ MREAIMQGKF KEFKREFYAK RGMI //