ID TGT_BACSU Reviewed; 381 AA. AC O32053; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 16-JUN-2009, entry version 63. 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=BSU27710; OS Bacillus subtilis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1423; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168; RA Tosato V., Bolotin A., Bertani I., Valentino I., Bruschi C.V.; RT "A 17.8 kb segment in the spoVB-nadC region of the Bacillus subtilis RT 168 chromosome: sequencing and ruv operon identification."; RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., RA Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., RA Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., RA Yoshikawa H., Danchin A.; RT "The complete genome sequence of the Gram-positive bacterium Bacillus RT subtilis."; RL Nature 390:249-256(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. 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; Y15896; CAB75333.1; -; Genomic_DNA. DR EMBL; AL009126; CAB14731.1; -; Genomic_DNA. DR PIR; B69722; B69722. DR RefSeq; NP_390649.1; -. DR HSSP; P28720; 1K4G. DR GeneID; 937528; -. DR GenomeReviews; AL009126_GR; BSU27710. DR KEGG; bsu:BSU27710; -. DR NMPDR; fig|224308.1.peg.2774; -. DR SubtiList; BG12686; tgt. DR HOGENOM; O32053; -. DR OMA; O32053; MAFDQCP. DR BioCyc; BSUB224308:BSU2767-MON; -. DR BRENDA; 2.4.2.29; 150. 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 1 381 Queuine tRNA-ribosyltransferase. FT /FTId=PRO_0000135452. FT ACT_SITE 96 96 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 97 97 Substrate (By similarity). SQ SEQUENCE 381 AA; 43711 MW; 76AD1B92883C6D36 CRC64; MAEQPIRYEF IKECKQTGAR LGKVHTPHGS FETPVFMPVG TLATVKTMSP EELKAMDAGI ILSNTYHLWL RPGQDIVKEA GGLHKFMNWD RAILTDSGGF QVFSLSKFRN IEEEGVHFRN HLNGDKLFLS PEKAMEIQNA LGSDIMMAFD ECPPYPAEYD YMKRSVERTS RWAERCLNAH NRQDEQGLFG IVQGGEYEDL RTQSAKDLIS LDFPGYAIGG LSVGEPKDVM NRVLEFTTPL LPKDKPRYLM GVGSPDALID GAIRGVDMFD CVLPTRIARN GTVFTAEGRL NMKNAKFERD FRPIDEECDC YTCKNYTRAY IRHLIRCNET FGLRLTTYHN LHFLLHLMEQ VRQAIREDRL GDFREEFFER YGYNKPNAKS F //