ATGT_METST
ID ATGT_METST Reviewed; 674 AA.
AC Q2NGY4;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=Msp_0520;
OS Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS MCB-3).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX NCBI_TaxID=339860;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3;
RX PubMed=16385054; DOI=10.1128/jb.188.2.642-658.2006;
RA Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA Gottschalk G., Thauer R.K.;
RT "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT intestinal archaeon is restricted to methanol and H2 for methane formation
RT and ATP synthesis.";
RL J. Bacteriol. 188:642-658(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; CP000102; ABC56919.1; -; Genomic_DNA.
DR RefSeq; WP_011406119.1; NC_007681.1.
DR AlphaFoldDB; Q2NGY4; -.
DR SMR; Q2NGY4; -.
DR STRING; 339860.Msp_0520; -.
DR EnsemblBacteria; ABC56919; ABC56919; Msp_0520.
DR GeneID; 41325094; -.
DR KEGG; mst:Msp_0520; -.
DR eggNOG; arCOG00989; Archaea.
DR eggNOG; arCOG00991; Archaea.
DR HOGENOM; CLU_030083_0_0_2; -.
DR OMA; FPCSCPV; -.
DR OrthoDB; 10236at2157; -.
DR UniPathway; UPA00393; -.
DR Proteomes; UP000001931; 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; 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; 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; Reference proteome; Transferase;
KW tRNA processing; Zinc.
FT CHAIN 1..674
FT /note="tRNA-guanine(15) transglycosylase"
FT /id="PRO_0000247876"
FT DOMAIN 596..671
FT /note="PUA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
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 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 674 AA; 77221 MW; 8FCDBB37860542D6 CRC64;
MVDIIVDFEI KYKDAMARVG KFKTPHGTVT TPALMPVVHP GKQTLDVKKL GAQIVITNSY
IIYKNEELKK KALEEGVHSL IDFPNTIETD SGSFQLSVYG DIDITNEEVI KFQEAIKTDI
GTSLDIPTAP YVKREEAEND LEITIERAKE AANVKSDLLL NSVVQGSTFP DLREKCAKEI
SKYDADIYPI GAVVPLMEMY RYADLVDAVM YSMRGLPENK PRHLMGAGHP MVFALATAMG
CDLFDSAAYI LYANKDRFMM PDGTLRLEDL IEMPCSCRVC CEYTVDELKQ MDQKKRAKLI
AEHNLHISFA EIRRIRQAIV DGELMKLVEL RCRSHPFLLD GLRRLMEYKE DMERLNPSSK
KSAFFYTGYE SLARSEVPKH LKQLENIKPK NKNLVILPHT RKPYTKYVNR EYIKKYTPKI
PTYYSNTTNT DYSNSDVVVA DIPFGIIPLG LDEFYPLAQN ESPSIHDLDS KRFIRDIINN
YSKKYDNVLI HRKVIEKFDI TNFNLIEDEL QLPEAKISDF NRLNDIADYQ FGCGAGNALF
GGDEDKITIE KSRKTKKIRH VFEDNENIVN MRANDGFLIL SDLGAKRLHK FLEYPHNRVV
VSEDSEPFAL KGKSVFNKFV LDCDENIRRN DEVLIVNKDD KLLAFGKALL SSYEIKDFNT
GQAIKTRKWK KEIE
