ID   TGT_AZOSB               Reviewed;         370 AA.
AC   A1K3W9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   16-JUN-2009, entry version 15.
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=azo0907;
OS   Azoarcus sp. (strain BH72).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Azoarcus.
OX   NCBI_TaxID=62928;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17057704; DOI=10.1038/nbt1243;
RA   Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J.,
RA   Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C.,
RA   Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J.,
RA   Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.;
RT   "Complete genome of the mutualistic, N2-fixing grass endophyte
RT   Azoarcus sp. strain BH72.";
RL   Nat. Biotechnol. 24:1385-1391(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; AM406670; CAL93524.1; -; Genomic_DNA.
DR   RefSeq; YP_932411.1; -.
DR   GeneID; 4606629; -.
DR   GenomeReviews; AM406670_GR; azo0907.
DR   KEGG; azo:azo0907; -.
DR   OMA; A1K3W9; 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    370       Queuine tRNA-ribosyltransferase.
FT                                /FTId=PRO_1000016762.
FT   ACT_SITE     89     89       Nucleophile (By similarity).
FT   METAL       302    302       Zinc (By similarity).
FT   METAL       304    304       Zinc (By similarity).
FT   METAL       307    307       Zinc (By similarity).
FT   METAL       333    333       Zinc (By similarity).
FT   BINDING      90     90       Substrate (By similarity).
SQ   SEQUENCE   370 AA;  40941 MW;  C2BD8C0FCB7EE874 CRC64;
     MQFELLSTSA GARRGRLTLA HGAVETPVFM PVGTYGTVKA MTPAMLSDVG AQICLGNTFH
     LWLRPGLDIV GAHGGLHRFM GWDKPILTDS GGFQVFSLGA LRKISEEGVK FASPIDGARL
     FLTPEISMQI QTVLNSDVVM IFDECTPYPA TRDEAAKSMR LSRRWARRSR DEFDRLENAN
     ALFGIVQGGM YEDLRDESLG ALQDIGFHGF AIGGLSVGEP KDDMARILAH TAPRLPADKP
     RYLMGVGTPE DIVDGIANGI DMFDCVMPTR NARNGWLFTR YGDLKIKNAV HKADTRPLDP
     SCSCYTCRNF SRSYLHHLHR AGEILGSMLN TVHNLHYYQT LTAELRDAIA ADRFADYVTR
     FRSERATGAH
//