ID   ATGT_METBF              Reviewed;         490 AA.
AC   Q46DI6;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=Mbar_A1088;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
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; CP000099; AAZ70056.1; -; Genomic_DNA.
DR   RefSeq; WP_011306104.1; NC_007355.1.
DR   AlphaFoldDB; Q46DI6; -.
DR   SMR; Q46DI6; -.
DR   STRING; 269797.Mbar_A1088; -.
DR   PRIDE; Q46DI6; -.
DR   EnsemblBacteria; AAZ70056; AAZ70056; Mbar_A1088.
DR   GeneID; 3627363; -.
DR   KEGG; mba:Mbar_A1088; -.
DR   eggNOG; arCOG00989; Archaea.
DR   HOGENOM; CLU_030083_0_0_2; -.
DR   OMA; FPCSCPV; -.
DR   OrthoDB; 10236at2157; -.
DR   UniPathway; UPA00393; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016763; F:pentosyltransferase activity; IEA:InterPro.
DR   GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR   Gene3D; 3.20.20.105; -; 1.
DR   HAMAP; MF_01634; TgtA_arch; 1.
DR   InterPro; IPR036511; TGT-like_sf.
DR   InterPro; IPR004804; TgtA.
DR   InterPro; IPR002616; tRNA_ribo_trans-like.
DR   Pfam; PF01702; TGT; 1.
DR   SUPFAM; SSF51713; SSF51713; 1.
DR   TIGRFAMs; TIGR00432; arcsn_tRNA_tgt; 1.
DR   TIGRFAMs; TIGR00449; tgt_general; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Metal-binding; Transferase; tRNA processing; Zinc.
FT   CHAIN           1..490
FT                   /note="tRNA-guanine(15) transglycosylase"
FT                   /id="PRO_0000247874"
FT   ACT_SITE        90
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT   BINDING         125
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT   BINDING         193
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT   BINDING         276
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"
FT   BINDING         281
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
SQ   SEQUENCE   490 AA;  55093 MW;  1BA449A86653D635 CRC64;
     MSAIFEILDK DAGGRIGRLR TPHGTVETPT VMPVINPNIQ LIPPKEMRNF GAEILITNSY
     IIYRKEELKS VALEKGLHGL LGFDGPIMTD SGSFQLSVYG SVEVTNEEIL GFQQKIGSDI
     IVPLDIPTPP DVHYRRAEEE LAITAERLEA ARKFIQSEQL LAGPVQGSTY PELREKAASH
     LKDLNFEVYP LGAVVPLMEA YRYAELVDVI AASKKGLSPA SPVHLFGAGH PMMFALAVAM
     GCDLFDSAAY ALYAKDGRYI TVNGTYHVEK LNYLPCSCPV CSKYTAEELK KADNREELLG
     KHNLYATFAE IRLIKQCIKD GKLLELVEQR CRAHPKLLDG LKKLYTHSSW LEQLDPATKG
     TFFYCGPESS SRPEILRFGK RLDRFSLQGS VIIRTGSVKG EKDYDQILTF KAPFGAFPVE
     MEEVYPFNAE VPKFPDYESL NTALSNTLKL IDLNPEAEFT FICEEEFKHP LIEEIRKRAK
     LVYRKDWKKE