(data stored in ACNUC7421 zone)

SWISSPROT: TGT_ECO27

ID   TGT_ECO27               Reviewed;         375 AA.
AC   B7UJM9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 58.
DE   RecName: Full=Queuine tRNA-ribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00168};
DE            EC=2.4.2.29 {ECO:0000255|HAMAP-Rule:MF_00168};
DE   AltName: Full=Guanine insertion enzyme {ECO:0000255|HAMAP-Rule:MF_00168};
DE   AltName: Full=tRNA-guanine transglycosylase {ECO:0000255|HAMAP-Rule:MF_00168};
GN   Name=tgt {ECO:0000255|HAMAP-Rule:MF_00168};
GN   OrderedLocusNames=E2348C_0341;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Catalyzes the base-exchange of a guanine (G) residue
CC       with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at
CC       position 34 (anticodon wobble position) in tRNAs with GU(N)
CC       anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs
CC       through a double-displacement mechanism. The nucleophile active
CC       site attacks the C1' of nucleotide 34 to detach the guanine base
CC       from the RNA, forming a covalent enzyme-RNA intermediate. The
CC       proton acceptor active site deprotonates the incoming PreQ1,
CC       allowing a nucleophilic attack on the C1' of the ribose to form
CC       the product. After dissociation, two additional enzymatic
CC       reactions on the tRNA convert PreQ1 to queuine (Q), resulting in
CC       the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-
CC       cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
CC       {ECO:0000255|HAMAP-Rule:MF_00168}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7-aminomethyl-7-carbaguanine + guanosine(34) in tRNA = 7-
CC         aminomethyl-7-carbaguanosine(34) in tRNA + guanine;
CC         Xref=Rhea:RHEA:24104, Rhea:RHEA-COMP:10341, Rhea:RHEA-
CC         COMP:10342, ChEBI:CHEBI:16235, ChEBI:CHEBI:58703,
CC         ChEBI:CHEBI:74269, ChEBI:CHEBI:82833; EC=2.4.2.29;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00168};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00168};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00168};
CC   -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00168}.
CC   -!- SUBUNIT: Homodimer. Within each dimer, one monomer is responsible
CC       for RNA recognition and catalysis, while the other monomer binds
CC       to the replacement base PreQ1. {ECO:0000255|HAMAP-Rule:MF_00168}.
CC   -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00168}.
DR   EMBL; FM180568; CAS07889.1; -; Genomic_DNA.
DR   RefSeq; WP_000667319.1; NC_011601.1.
DR   SMR; B7UJM9; -.
DR   EnsemblBacteria; CAS07889; CAS07889; E2348C_0341.
DR   KEGG; ecg:E2348C_0341; -.
DR   KO; K00773; -.
DR   OMA; GIDLFDC; -.
DR   BioCyc; ECOL574521:E2348C_RS01795-MONOMER; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008479; F:queuine tRNA-ribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0101030; P:tRNA-guanine transglycosylation; IEA:InterPro.
DR   Gene3D; 3.20.20.105; -; 1.
DR   HAMAP; MF_00168; Q_tRNA_Tgt; 1.
DR   InterPro; IPR004803; TGT.
DR   InterPro; IPR036511; TGT-like_sf.
DR   InterPro; IPR002616; tRNA_ribo_trans-like.
DR   Pfam; PF01702; TGT; 1.
DR   SUPFAM; SSF51713; SSF51713; 1.
DR   TIGRFAMs; TIGR00430; Q_tRNA_tgt; 1.
DR   TIGRFAMs; TIGR00449; tgt_general; 1.
PE   3: Inferred from homology;
DR   PRODOM; B7UJM9.
DR   SWISS-2DPAGE; B7UJM9.
KW   Complete proteome; Glycosyltransferase; Metal-binding;
KW   Queuosine biosynthesis; Transferase; tRNA processing; Zinc.
FT   CHAIN         1    375       Queuine tRNA-ribosyltransferase.
FT                                /FTId=PRO_1000198002.
FT   REGION       89     93       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00168}.
FT   REGION      245    251       RNA binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00168}.
FT   REGION      269    273       RNA binding; important for wobble base 34
FT                                recognition. {ECO:0000255|HAMAP-
FT                                Rule:MF_00168}.
FT   ACT_SITE     89     89       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00168}.
FT   ACT_SITE    264    264       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_00168}.
FT   METAL       302    302       Zinc. {ECO:0000255|HAMAP-Rule:MF_00168}.
FT   METAL       304    304       Zinc. {ECO:0000255|HAMAP-Rule:MF_00168}.
FT   METAL       307    307       Zinc. {ECO:0000255|HAMAP-Rule:MF_00168}.
FT   METAL       333    333       Zinc; via pros nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00168}.
FT   BINDING     143    143       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00168}.
FT   BINDING     187    187       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00168}.
FT   BINDING     214    214       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00168}.
SQ   SEQUENCE   375 AA;  42594 MW;  40271CA08D8A8820 CRC64;
     MKFELDTTDG RARRGRLVFD RGVVETPCFM PVGTYGTVKG MTPEEVEATG AQIILGNTFH
     LWLRPGQEIM KLHGDLHDFM QWKGPILTDS GGFQVFSLGD IRKITEQGVH FRNPINGDPI
     FLDPEKSMEI QYDLGSDIVM IFDECTPYPA DWDYAKRSME MSLRWAKRSR ERFDSLGNKN
     ALFGIIQGSV YEDLRDISVK GLVDIGFDGY AVGGLAVGEP KADMHRILEH VCPQIPADKP
     RYLMGVGKPE DLVEGVRRGI DMFDCVMPTR NARNGHLFVT DGVVKIRNAK YKSDTGPLDP
     ECDCYTCRNY SRAYLHHLDR CNEILGARLN TIHNLRYYQR LMAGLRKAIE EGKLESFVTD
     FYQRQGREVP PLNVD
//

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