ATGT_METS3
ID ATGT_METS3 Reviewed; 659 AA.
AC A5UNI4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=Msm_1557;
OS Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=420247;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT human gut.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
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; CP000678; ABQ87762.1; -; Genomic_DNA.
DR RefSeq; WP_011954592.1; NC_009515.1.
DR AlphaFoldDB; A5UNI4; -.
DR SMR; A5UNI4; -.
DR STRING; 420247.Msm_1557; -.
DR EnsemblBacteria; ABQ87762; ABQ87762; Msm_1557.
DR GeneID; 5216721; -.
DR KEGG; msi:Msm_1557; -.
DR PATRIC; fig|420247.28.peg.1547; -.
DR eggNOG; arCOG00989; Archaea.
DR eggNOG; arCOG00991; Archaea.
DR HOGENOM; CLU_030083_0_0_2; -.
DR OMA; FPCSCPV; -.
DR UniPathway; UPA00393; -.
DR Proteomes; UP000001992; 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 Gene3D; 2.30.130.10; -; 1.
DR Gene3D; 3.10.450.90; -; 1.
DR Gene3D; 3.20.20.105; -; 1.
DR HAMAP; MF_01634; TgtA_arch; 1.
DR InterPro; IPR040777; DUF5591.
DR InterPro; IPR002478; PUA.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR036974; PUA_sf.
DR InterPro; IPR036511; TGT-like_sf.
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 Pfam; PF17884; DUF5591; 1.
DR Pfam; PF01472; PUA; 1.
DR Pfam; PF01702; TGT; 1.
DR Pfam; PF14810; TGT_C2; 1.
DR SMART; SM00359; PUA; 1.
DR SUPFAM; SSF51713; SSF51713; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR00432; arcsn_tRNA_tgt; 1.
DR TIGRFAMs; TIGR00449; tgt_general; 1.
DR TIGRFAMs; TIGR00451; unchar_dom_2; 1.
DR PROSITE; PS50890; PUA; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Metal-binding; Transferase; tRNA processing; Zinc.
FT CHAIN 1..659
FT /note="tRNA-guanine(15) transglycosylase"
FT /id="PRO_0000335807"
FT DOMAIN 583..658
FT /note="PUA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT ACT_SITE 84
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT BINDING 273
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
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 278
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
SQ SEQUENCE 659 AA; 74780 MW; 16110AE6088B176F CRC64;
MFEIKAKDNR GRVGVLKTNS GDVKTPNLMP VIHPRKQTID VKKYGADIVI TNAYLIYKDE
DLKKKAAEIG LHKLINFDGP IMTDSGSFQL SVYGDVDITN KEVIEFQELI KTDIGTSLDI
PTAPFVTREK AEADLEVTLE RAKEAVDYRN SQNMEMKLNS VVQGSTFPDL RRKCADELTK
LDADLYPIGA VVPLMESYHY KELVDVVMNS VAHLPDSKPR HLMGAGHPMI FALAVAMGCD
LFDSAAYILY AEDDRLLSVR GTYKLENLQE MPCSCEVCCN YTPDDLRAMP KEKRRDLIAQ
HNLNVSFAEL RLIRQAIYEG SLMELVEERC RAHPNLLEAL RQLGNYSKDL EKYDPRSKKS
AFFYTGSESL YRSEVLRHIQ KLRAMPRKRD LVILPPSRKP YSKYVSSKLG NFYVYGSEQE
LDLNNTDFMV LDIPFGLIPL EIDEIYPLSQ NESPRTWDVS SLEFIEDFIS EFVEYYDQVL
IHSNVIKKLD IGLYNIHSQS DEIRYAKDDL KKVKAIADYQ FGVGAGDALF AGNIKIEKSK
KTGKIRHIYD GKTLIVNMRA SDSFLILSKE GAKRLHAATQ YPKNRVVVNK DSEPFSLEGK
SVFAKFVVEC DEDIRAKDEV LIVNEEDKLL AYGKALLGAC EINDFQTGQA IKTRKGMKK
