ID ATGT_THEON Reviewed; 580 AA.
AC B6YUR8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=tRNA-guanine(15) transglycosylase {ECO:0000255|HAMAP-Rule:MF_01634};
DE EC=2.4.2.48 {ECO:0000255|HAMAP-Rule:MF_01634};
DE AltName: Full=7-cyano-7-deazaguanine tRNA-ribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01634};
DE AltName: Full=Archaeal tRNA-guanine transglycosylase {ECO:0000255|HAMAP-Rule:MF_01634};
GN Name=tgtA {ECO:0000255|HAMAP-Rule:MF_01634}; OrderedLocusNames=TON_0617;
OS Thermococcus onnurineus (strain NA1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=523850;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1;
RX PubMed=18790866; DOI=10.1128/jb.00746-08;
RA Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H.,
RA Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J.,
RA Colwell R.R., Kim S.-J., Lee J.-H.;
RT "The complete genome sequence of Thermococcus onnurineus NA1 reveals a
RT mixed heterotrophic and carboxydotrophic metabolism.";
RL J. Bacteriol. 190:7491-7499(2008).
CC -!- FUNCTION: Exchanges the guanine residue with 7-cyano-7-deazaguanine
CC (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal
CC tRNAs. {ECO:0000255|HAMAP-Rule:MF_01634}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-
CC carbaguanosine(15) in tRNA + guanine; Xref=Rhea:RHEA:43164,
CC Rhea:RHEA-COMP:10371, Rhea:RHEA-COMP:10372, ChEBI:CHEBI:16235,
CC ChEBI:CHEBI:45075, ChEBI:CHEBI:74269, ChEBI:CHEBI:82850; EC=2.4.2.48;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01634};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01634};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01634};
CC -!- PATHWAY: tRNA modification; archaeosine-tRNA biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01634}.
CC -!- SIMILARITY: Belongs to the archaeosine tRNA-ribosyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_01634}.
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DR EMBL; CP000855; ACJ16104.1; -; Genomic_DNA.
DR RefSeq; WP_012571576.1; NC_011529.1.
DR AlphaFoldDB; B6YUR8; -.
DR SMR; B6YUR8; -.
DR STRING; 523850.TON_0617; -.
DR GeneID; 7016915; -.
DR KEGG; ton:TON_0617; -.
DR PATRIC; fig|523850.10.peg.618; -.
DR eggNOG; arCOG00989; Archaea.
DR eggNOG; arCOG00991; Archaea.
DR HOGENOM; CLU_030083_0_0_2; -.
DR OrthoDB; 6871at2157; -.
DR UniPathway; UPA00393; -.
DR Proteomes; UP000002727; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016763; F:pentosyltransferase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR CDD; cd21149; PUA_archaeosine_TGT; 1.
DR Gene3D; 3.90.1020.10; ArcTGT, C1 domain; 1.
DR Gene3D; 3.10.450.90; ArcTGT, C2 domain; 1.
DR Gene3D; 2.30.130.10; PUA domain; 1.
DR Gene3D; 3.20.20.105; Queuine tRNA-ribosyltransferase-like; 1.
DR HAMAP; MF_01634; TgtA_arch; 1.
DR InterPro; IPR038370; ArcTGT_C1_sf.
DR InterPro; IPR002478; PUA.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR036974; PUA_sf.
DR InterPro; IPR036511; TGT-like_sf.
DR InterPro; IPR032729; TGT_C1.
DR InterPro; IPR029402; TGT_C2.
DR InterPro; IPR038250; TGT_C2_sf.
DR InterPro; IPR004804; TgtA.
DR InterPro; IPR002616; tRNA_ribo_trans-like.
DR InterPro; IPR004521; Uncharacterised_CHP00451.
DR NCBIfam; TIGR00432; arcsn_tRNA_tgt; 1.
DR NCBIfam; TIGR00449; tgt_general; 1.
DR NCBIfam; TIGR00451; unchar_dom_2; 1.
DR PANTHER; PTHR46499; QUEUINE TRNA-RIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR46499:SF1; QUEUINE TRNA-RIBOSYLTRANSFERASE; 1.
DR Pfam; PF01472; PUA; 1.
DR Pfam; PF01702; TGT; 1.
DR Pfam; PF14809; TGT_C1; 1.
DR Pfam; PF14810; TGT_C2; 1.
DR SMART; SM00359; PUA; 1.
DR SUPFAM; SSF88802; Pre-PUA domain; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF51713; tRNA-guanine transglycosylase; 1.
DR PROSITE; PS50890; PUA; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Metal-binding; Transferase; tRNA processing; Zinc.
FT CHAIN 1..580
FT /note="tRNA-guanine(15) transglycosylase"
FT /id="PRO_1000186652"
FT DOMAIN 504..579
FT /note="PUA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT ACT_SITE 91
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT BINDING 275
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT BINDING 277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
SQ SEQUENCE 580 AA; 66172 MW; 3265E7244D8F117A CRC64;
MVEFKFEVKA RDAAGRIGKL EVNGKKIETP AIMPVINPKQ LTVTPKELKE MGFGIIITNS
YIIYKTPELR EKALEVGIHR LLDYDGIIEV DSGSFQLMRY GGVDVTNREI VEFQERIGVD
IGTFLDIPTP PDAPREKAEE DLRITLERAK EAEEIKGIAM NAAVQGSTYP DLRTYAARKL
SEMNFEIHPI GAVVPLMESY RYRDLVDVVI ASKQGLRSDR PVHLFGAGHP MIFALAVAMG
IDLFDSASYA LYAKDDRYLT PEGTKHLSEL EYFPCSCPVC SRYTPRELRE MPKEERTRLL
ALHNLWVIRE ELNRVKQAIK EGELWRLVDE RARSHPKLYA AYKRLLEYQD YLEKNEPITK
ASAFFKVSEE SLKWPIVQRA KARAERVKAK FPETINHPIF GEIPKYLSLS YPFAQSEGEE
DFTIEKPGKR EVRNYVMAVA EYQFGEGTRE AFKDAFVELS RKTGMPRQIK AKGKHLATFR
AEDGLLTLGI EGAKRLHEIL PFPRMRVVVD EDAEPFARKG KNVFAKFVID ADENIRPYDE
VLIVNRNDEL LATGQTLLNG RELKLFQSGL AVKVRRGVEK
//
