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Database: UniProt
Entry: B5ZPR9_RHILW
LinkDB: B5ZPR9_RHILW
Original site: B5ZPR9_RHILW 
ID   B5ZPR9_RHILW            Unreviewed;       376 AA.
AC   B5ZPR9;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   24-JAN-2024, entry version 120.
DE   RecName: Full=Queuine tRNA-ribosyltransferase {ECO:0000256|HAMAP-Rule:MF_00168};
DE            EC=2.4.2.29 {ECO:0000256|HAMAP-Rule:MF_00168};
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   OrderedLocusNames=Rleg2_1752 {ECO:0000313|EMBL:ACI55039.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM2304).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395492 {ECO:0000313|EMBL:ACI55039.1, ECO:0000313|Proteomes:UP000008330};
RN   [1] {ECO:0000313|EMBL:ACI55039.1, ECO:0000313|Proteomes:UP000008330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM2304 {ECO:0000313|EMBL:ACI55039.1,
RC   ECO:0000313|Proteomes:UP000008330};
RX   PubMed=21304679; DOI=10.4056/sigs.44642;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., Tiwari R.,
RA   Malfatti S., Kiss H., Lapidus A., Copeland A., Nolan M., Land M.,
RA   Ivanova N., Mavromatis K., Markowitz V., Kyrpides N., Melino V., Denton M.,
RA   Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv trifolii strain
RT   WSM2304, an effective microsymbiont of the South American clover Trifolium
RT   polymorphum.";
RL   Stand. Genomic Sci. 2:66-76(2010).
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:0000256|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:0000256|HAMAP-
CC         Rule:MF_00168};
CC   -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC       {ECO:0000256|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:0000256|HAMAP-Rule:MF_00168}.
CC   -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00168}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00168}.
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DR   EMBL; CP001191; ACI55039.1; -; Genomic_DNA.
DR   RefSeq; WP_012557668.1; NC_011369.1.
DR   AlphaFoldDB; B5ZPR9; -.
DR   STRING; 395492.Rleg2_1752; -.
DR   KEGG; rlt:Rleg2_1752; -.
DR   eggNOG; COG0343; Bacteria.
DR   HOGENOM; CLU_022060_0_1_5; -.
DR   OMA; GIDLFDC; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000008330; Chromosome.
DR   GO; GO:0008479; F:tRNA-guanosine(34) queuine transglycosylase 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; Queuine tRNA-ribosyltransferase-like; 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   NCBIfam; TIGR00430; Q_tRNA_tgt; 1.
DR   NCBIfam; TIGR00449; tgt_general; 1.
DR   PANTHER; PTHR46499; QUEUINE TRNA-RIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR46499:SF1; QUEUINE TRNA-RIBOSYLTRANSFERASE; 1.
DR   Pfam; PF01702; TGT; 1.
DR   SUPFAM; SSF51713; tRNA-guanine transglycosylase; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW   Rule:MF_00168}; Queuosine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00168};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00168};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_00168}.
FT   DOMAIN          15..369
FT                   /note="tRNA-guanine(15) transglycosylase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01702"
FT   REGION          248..254
FT                   /note="RNA binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   REGION          272..276
FT                   /note="RNA binding; important for wobble base 34
FT                   recognition"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   ACT_SITE        93
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   ACT_SITE        267
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   BINDING         93..97
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   BINDING         147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   BINDING         190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
FT   BINDING         217
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00168"
SQ   SEQUENCE   376 AA;  41737 MW;  4AC762F62F9D088D CRC64;
     MTENFQFTLK KTDAGARLGE ISMPRGTIRT PAFMPVGTVG TVKAMYLDQV RETGADIILG
     NTYHLMLRPS AERVARLGGL HKLIRWEHPI LTDSGGFQVM SLSGLRKLDE QGVTFKSHVD
     GSLHHMSPER SIEIQGLLGS DIQMQLDECV ALPAEPREIE RAMEMSLRWA ERCRVAFGEQ
     PGKAMFGIVQ GGDIPALRVR SAQALSELDL KGYAIGGLAV GEPQDVMLQM LDTTLPVLPG
     EKPRYLMGVG TPDDILKSVA RGIDMFDCVM PTRSGRHGLA FTRRGKVNIR NARHAEDMRP
     LDDQSNCPAS RDYSRAYLHH LVRSNEALGG MLLSWNNLAY YQELMQGIRK AIAEGRFADF
     MAETMEEWAR GDLDPV
//
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