(data stored in ACNUC7421 zone)

SWISSPROT: Q145I0_PARXL

ID   Q145I0_PARXL            Unreviewed;       396 AA.
AC   Q145I0;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 103.
DE   RecName: Full=Queuine tRNA-ribosyltransferase {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00087750};
DE            EC=2.4.2.29 {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00087822};
DE   AltName: Full=Guanine insertion enzyme {ECO:0000256|HAMAP-Rule:MF_00168};
DE   AltName: Full=tRNA-guanine transglycosylase {ECO:0000256|HAMAP-Rule:MF_00168};
GN   Name=tgt {ECO:0000256|HAMAP-Rule:MF_00168};
GN   ORFNames=Bxe_A3990 {ECO:0000313|EMBL:ABE29009.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE29009.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE29009.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE29009.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777,
CC       ECO:0000256|SAAS:SAAS00628203}.
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:0000256|HAMAP-Rule:MF_00168,
CC         ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS01115764};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00168, ECO:0000256|RuleBase:RU003777};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00168, ECO:0000256|RuleBase:RU003777};
CC   -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|SAAS:SAAS00087869}.
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:0000256|HAMAP-Rule:MF_00168,
CC       ECO:0000256|SAAS:SAAS00628204}.
CC   -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777,
CC       ECO:0000256|SAAS:SAAS00571098}.
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DR   EMBL; CP000270; ABE29009.1; -; Genomic_DNA.
DR   RefSeq; WP_011486832.1; NZ_CP008760.1.
DR   STRING; 266265.Bxe_A3990; -.
DR   EnsemblBacteria; ABE29009; ABE29009; Bxe_A3990.
DR   GeneID; 4002085; -.
DR   KEGG; bxb:DR64_1667; -.
DR   KEGG; bxe:Bxe_A3990; -.
DR   PATRIC; fig|266265.5.peg.497; -.
DR   eggNOG; ENOG4105C6U; Bacteria.
DR   eggNOG; COG0343; LUCA.
DR   HOGENOM; HOG000223473; -.
DR   KO; K00773; -.
DR   OMA; GIDLFDC; -.
DR   OrthoDB; 1165356at2; -.
DR   BioCyc; BXEN266265:BXE_RS02360-MONOMER; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000001817; Chromosome 1.
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; Q145I0.
DR   SWISS-2DPAGE; Q145I0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00168,
KW   ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00460875,
KW   ECO:0000313|EMBL:ABE29009.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00168,
KW   ECO:0000256|SAAS:SAAS00101950};
KW   Queuosine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00168,
KW   ECO:0000256|SAAS:SAAS00460855};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00168,
KW   ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00876991,
KW   ECO:0000313|EMBL:ABE29009.1};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00168,
KW   ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00460804};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777,
KW   ECO:0000256|SAAS:SAAS00087669}.
FT   DOMAIN       29    389       TGT. {ECO:0000259|Pfam:PF01702}.
FT   REGION      107    111       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00168}.
FT   REGION      268    274       RNA binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00168}.
FT   REGION      292    296       RNA binding; important for wobble base 34
FT                                recognition. {ECO:0000256|HAMAP-Rule:
FT                                MF_00168}.
FT   ACT_SITE    107    107       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00168}.
FT   ACT_SITE    287    287       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_00168}.
FT   METAL       325    325       Zinc. {ECO:0000256|HAMAP-Rule:MF_00168}.
FT   METAL       327    327       Zinc. {ECO:0000256|HAMAP-Rule:MF_00168}.
FT   METAL       330    330       Zinc. {ECO:0000256|HAMAP-Rule:MF_00168}.
FT   METAL       356    356       Zinc; via pros nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00168}.
FT   BINDING     161    161       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00168}.
FT   BINDING     210    210       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00168}.
FT   BINDING     237    237       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00168}.
SQ   SEQUENCE   396 AA;  44305 MW;  2F099B8A9A7E1FC5 CRC64;
     MTDGHLSQDA THERPENGLK FELLGVDGQA RRGRVALNHG VVETPIFMPV GTYGTVKAVQ
     PRELEEMHAQ IILGNTFHLW LRPGLETIEA YGGLHGFMGW KKPILTDSGG FQVFSLGDLR
     KITEDGVTFA SPINGDKLFL SPEVSMQIQK VLNSDIVMQF DECTPYATHN VPTSHQEAAD
     SMRMSMRWAQ RSIDEFNRLG NPNALFGIVQ GGMFEDLRDE SLAGLAEKDF HGLAIGGLSV
     GEPKEDMMRV LNHIGPKLPA NKPHYLMGVG TPEDLVAGVA AGVDMFDCVM PTRNARNGWL
     FTRFGDIKIR NAAHRNSLRP LDEQCGCYTC RNFTRGYLHH LHRVGEILGA QLNTIHNLHY
     YLELMQEIRD AIDAKMFEPF RKRFHENRAR GTAEAP
//

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