(data stored in ACNUC7421 zone)

SWISSPROT: TGT_PSEHT

ID   TGT_PSEHT               Reviewed;         375 AA.
AC   Q3ILB8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   05-JUL-2017, entry version 81.
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=PSHAa0319;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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: Guanine(34) in tRNA + 7-aminomethyl-7-
CC       carbaguanine = 7-aminomethyl-7-carbaguanine(34) in tRNA + guanine.
CC       {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; CR954246; CAI85418.1; -; Genomic_DNA.
DR   RefSeq; WP_011327032.1; NC_007481.1.
DR   ProteinModelPortal; Q3ILB8; -.
DR   SMR; Q3ILB8; -.
DR   STRING; 326442.PSHAa0319; -.
DR   EnsemblBacteria; CAI85418; CAI85418; PSHAa0319.
DR   GeneID; 32565692; -.
DR   KEGG; pha:PSHAa0319; -.
DR   eggNOG; ENOG4105C6U; Bacteria.
DR   eggNOG; COG0343; LUCA.
DR   HOGENOM; HOG000223473; -.
DR   KO; K00773; -.
DR   OMA; TYHLFLR; -.
DR   OrthoDB; POG091H00XO; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008479; F:queuine tRNA-ribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-UniPathway.
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; 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; Q3ILB8.
DR   SWISS-2DPAGE; Q3ILB8.
KW   Complete proteome; Glycosyltransferase; Metal-binding;
KW   Queuosine biosynthesis; Reference proteome; Transferase;
KW   tRNA processing; Zinc.
FT   CHAIN         1    375       Queuine tRNA-ribosyltransferase.
FT                                /FTId=PRO_1000016829.
FT   REGION       89     93       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00168}.
FT   REGION      243    249       RNA binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00168}.
FT   REGION      267    271       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    262    262       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_00168}.
FT   METAL       300    300       Zinc. {ECO:0000255|HAMAP-Rule:MF_00168}.
FT   METAL       302    302       Zinc. {ECO:0000255|HAMAP-Rule:MF_00168}.
FT   METAL       305    305       Zinc. {ECO:0000255|HAMAP-Rule:MF_00168}.
FT   METAL       331    331       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     185    185       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00168}.
FT   BINDING     212    212       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00168}.
SQ   SEQUENCE   375 AA;  41722 MW;  EBA2BD4DFACA1C56 CRC64;
     MKFELDTTDG KARRGRLIFD RGVIETPAFM PVGTYGTVKG MTPDEVKATG AQVCLGNTFH
     LMLRPGTEII KQHGGLHKFM NWDFPILTDS GGFQVFSLGA MRKITEEGVL FSSPVNGEKI
     MMTPESSMQV QRDLGSDIVM IFDECTPYPA TEKEAKDSME LSLRWAKRSK EGHGDNPSAL
     FGIIQGGMYP ELRAQSQAGL EEIGFDGYAL GGLSVGEPKN EMINILDHCA YKMPADKPRY
     LMGVGKPEDL VESVRRGIDM FDCVMPTRNA RNGHLFITTG VVKIRNAVHK TDTGPLDPEC
     DCHTCGNYSR AYLHHLDKCN EILGARLNTI HNLRYYQRVM EGLRNAISAG KLDEFVQDFY
     ARRGQDVPEL ADITN
//

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