(data stored in SCRATCH3701 zone)

SWISSPROT: TGT_SYNS3

ID   TGT_SYNS3               Reviewed;         372 AA.
AC   Q0IDF3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   11-DEC-2019, entry version 84.
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}; OrderedLocusNames=sync_0284;
OS   Synechococcus sp. (strain CC9311).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=64471;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9311;
RX   PubMed=16938853; DOI=10.1073/pnas.0602963103;
RA   Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H.,
RA   Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S.,
RA   Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R.,
RA   Paulsen I.T.;
RT   "Genome sequence of Synechococcus CC9311: insights into adaptation to a
RT   coastal environment.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006).
CC   -!- FUNCTION: Catalyzes the base-exchange of a guanine (G) residue with the
CC       queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34
CC       (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp,
CC       -Asn, -His and -Tyr). Catalysis occurs through a double-displacement
CC       mechanism. The nucleophile active site attacks the C1' of nucleotide 34
CC       to detach the guanine base from the RNA, forming a covalent enzyme-RNA
CC       intermediate. The proton acceptor active site deprotonates the incoming
CC       PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form
CC       the product. After dissociation, two additional enzymatic reactions on
CC       the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified
CC       nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-
CC       yl)amino)methyl)-7-deazaguanosine). {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-COMP:10342,
CC         ChEBI:CHEBI:16235, ChEBI:CHEBI:58703, ChEBI:CHEBI:74269,
CC         ChEBI:CHEBI:82833; EC=2.4.2.29; Evidence={ECO:0000255|HAMAP-
CC         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-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 for
CC       RNA recognition and catalysis, while the other monomer binds to the
CC       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; CP000435; ABI46127.1; -; Genomic_DNA.
DR   RefSeq; WP_011618264.1; NC_008319.1.
DR   SMR; Q0IDF3; -.
DR   STRING; 64471.sync_0284; -.
DR   EnsemblBacteria; ABI46127; ABI46127; sync_0284.
DR   KEGG; syg:sync_0284; -.
DR   eggNOG; ENOG4105C6U; Bacteria.
DR   eggNOG; COG0343; LUCA.
DR   HOGENOM; HOG000223473; -.
DR   KO; K00773; -.
DR   OMA; GIDLFDC; -.
DR   OrthoDB; 1165356at2; -.
DR   BioCyc; SSP64471:G1G72-276-MONOMER; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000001961; 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; Q0IDF3.
DR   SWISS-2DPAGE; Q0IDF3.
KW   Glycosyltransferase; Metal-binding; Queuosine biosynthesis;
KW   Reference proteome; Transferase; tRNA processing; Zinc.
FT   CHAIN           1..372
FT                   /note="Queuine tRNA-ribosyltransferase"
FT                   /id="PRO_1000016881"
FT   REGION          92..96
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT   REGION          246..252
FT                   /note="RNA binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT   REGION          270..274
FT                   /note="RNA binding; important for wobble base 34
FT                   recognition"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT   ACT_SITE        92
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT   ACT_SITE        265
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT   METAL           303
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT   METAL           305
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT   METAL           308
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT   METAL           334
FT                   /note="Zinc; via pros nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT   BINDING         146
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT   BINDING         188
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
FT   BINDING         215
FT                   /note="Substrate; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00168"
SQ   SEQUENCE   372 AA;  41034 MW;  1E02ACE5CE83FA30 CRC64;
     MFQFEIQATC SNTGARCGCF HTPHGPVTTP RFMPVGTLGT VKGVTTSQLA ETGAQMVLSN
     TYHLHLQPGE EIVADAGGLH RFMGWDGPML TDSGGFQVFS LGDLNRIDDE GVDFRNPRNG
     SRILLTPERS MQIQMRLGAD VAMAFDQCPP YPATENDVAE ACRRTHAWLG RCADAHQRDD
     QALFGIVQGG CFPHLRDLSA RTVASFNLPG IAIGGVSVGE PVEEMHQIVR QVTPLLPADR
     PRYLMGIGTL REMAVAVANG IDMFDCVLPT RLGRHGTALV GGERWNLRNA RFRHDHTPLD
     PNCPCIACRQ HTRAYLHHLI RSEELLGLTL LSIHNLTHLI RFTTAMGQAI RDGCFSEDFA
     PWEPSSRAHH TW
//

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