ID TGT_CLOPS Reviewed; 380 AA. AC Q0SRN5; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 16-JUN-2009, entry version 21. 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=CPR_1912; OS Clostridium perfringens (strain SM101 / Type A). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=289380; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16825665; DOI=10.1101/gr.5238106; RA Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., RA DeBoy R.T., Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., RA Haft D.H., Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., RA Sullivan S.A., Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., RA Benton J., Radune D., Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., RA Billington S.J., Songer J.G., McClane B.A., Titball R.W., Rood J.I., RA Melville S.B., Paulsen I.T.; RT "Skewed genomic variability in strains of the toxigenic bacterial RT pathogen, Clostridium perfringens."; RL Genome Res. 16:1031-1040(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. 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; CP000312; ABG87624.1; -; Genomic_DNA. DR RefSeq; YP_699222.1; -. DR GeneID; 4206159; -. DR GenomeReviews; CP000312_GR; CPR_1912. DR KEGG; cpr:CPR_1912; -. DR TIGR; CPR_1912; -. DR HOGENOM; Q0SRN5; -. DR OMA; Q0SRN5; 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 1 380 Queuine tRNA-ribosyltransferase. FT /FTId=PRO_1000016783. FT ACT_SITE 93 93 Nucleophile (By similarity). FT METAL 313 313 Zinc (By similarity). FT METAL 315 315 Zinc (By similarity). FT METAL 318 318 Zinc (By similarity). FT METAL 344 344 Zinc (By similarity). FT BINDING 94 94 Substrate (By similarity). SQ SEQUENCE 380 AA; 43186 MW; 113B6B73540539D6 CRC64; MTKKRYTLLK KDGKARRGEF VTPHGTIQTP VFMNVGTLAA IKGAVSSMDL KEIGCQVELS NTYHLHLRPG DKIVKQMGGL HNFMNWDRPI LTDSGGFQVF SLAGMRKIKE EGVYFNSHID GRKIFMGPEE SMQIQSNLGS TIAMAFDECI PNPSTREYVE KSVARTTRWL ERCKKEMDRL NSLDDTVNKE QMLFGINQGG VYEDIRIEHA KTIREMDLDG YAIGGLAVGE THEEMYRVID AVVPHLPEDK PIYLMGVGLP SNILEAVERG VDFFDCVLPA RNGRHGHVFT KEGKINLMNA KFELDARPID EGCQCPACKN YTRAYIRHLF KAKEMLAMRL CVLHNLYFYN KLMEDIRDAI DGGYFAEFKA KKLEEWNGRA //