ID TGT_CAMC1 Reviewed; 376 AA. AC A7ZD89; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 1. DT 16-JUN-2009, entry version 10. 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=Ccon26_08790; ORFNames=CCC13826_0093; OS Campylobacter concisus (strain 13826). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=360104; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., RA Mandrell R.E., On S., Nelson K.E.; RT "Genome sequence of Campylobacter concisus 13826 isolated from human RT feces."; RL Submitted (OCT-2007) 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; CP000792; EAT97330.1; -; Genomic_DNA. DR RefSeq; YP_001466747.1; -. DR GeneID; 5596725; -. DR GenomeReviews; CP000792_GR; Ccon26_08790. DR KEGG; cco:CCC13826_0093; -. DR OMA; A7ZD89; 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 1 376 Queuine tRNA-ribosyltransferase. FT /FTId=PRO_1000016767. 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 376 AA; 42535 MW; 15FAE716F34D1F73 CRC64; MKFEVIKKDG NARRGILTTA HSVIQTPVFM PVGTVGAVKS LDAFDMSEIL DAKIILANTY HMYLRPGSKV VREFGGLHGF SKFDRSFLTD SGGFQAFSLR SNTKNDDGGI KFKSHIDGST HYFTPRSVLD TQYELGSDIM MILDDLVALP AEPKRIDLSI KRTIKWAKEA IDYHKFMQSK GVGLQQNIFG IVQGGTDYEA RKFCAEALNE MPFDGLAIGG LSVGESNEAM YDTVEAVMPF MDELRPRYLM GVGTPEDLVE NVERGVDMFD CVMPTRNARN GTLFTSFGKI NIKSAKFIND HAPIDPQCQC YTCKRYSRGY LNHLFKAREL TFFRLASLHN LHYYLNLMKE MREAIEVGEF AKFKRNFYAK RSTDEL //