ATGT_PYRFU
ID ATGT_PYRFU Reviewed; 585 AA.
AC Q8TH08;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=tRNA-guanine(15) transglycosylase {ECO:0000255|HAMAP-Rule:MF_01634};
DE EC=2.4.2.48 {ECO:0000269|PubMed:16407303};
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=PF1046;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, INFLUENCE OF C-TERMINAL EXTENSION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16407303; DOI=10.1074/jbc.m512841200;
RA Sabina J., Soell D.;
RT "The RNA-binding PUA domain of archaeal tRNA-guanine transglycosylase is
RT not required for archaeosine formation.";
RL J. Biol. Chem. 281:6993-7001(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:0000269|PubMed:16407303}.
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:0000269|PubMed:16407303};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.16 uM for tRNA-Asp {ECO:0000269|PubMed:16407303};
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; AE009950; AAL81170.1; -; Genomic_DNA.
DR RefSeq; WP_011012183.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8TH08; -.
DR SMR; Q8TH08; -.
DR IntAct; Q8TH08; 1.
DR STRING; 186497.PF1046; -.
DR EnsemblBacteria; AAL81170; AAL81170; PF1046.
DR GeneID; 41712857; -.
DR KEGG; pfu:PF1046; -.
DR PATRIC; fig|186497.12.peg.1107; -.
DR eggNOG; arCOG00989; Archaea.
DR eggNOG; arCOG00991; Archaea.
DR HOGENOM; CLU_030083_0_0_2; -.
DR OMA; FPCSCPV; -.
DR OrthoDB; 10236at2157; -.
DR PhylomeDB; Q8TH08; -.
DR UniPathway; UPA00393; -.
DR Proteomes; UP000001013; 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 Gene3D; 3.90.1020.10; -; 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 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; 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 1: Evidence at protein level;
KW Glycosyltransferase; Metal-binding; Reference proteome; Transferase;
KW tRNA processing; Zinc.
FT CHAIN 1..585
FT /note="tRNA-guanine(15) transglycosylase"
FT /id="PRO_0000247616"
FT DOMAIN 507..582
FT /note="PUA"
FT ACT_SITE 95
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT BINDING 279
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"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
SQ SEQUENCE 585 AA; 66941 MW; 747CDCB3E147CC0A CRC64;
MSRGDSMLRF EIKDRDAAGR IGKLEVNGKK IETPAIMPVV NPKQLIVEPK ELKRMGFDII
ITNSYIIYKD KKLREKALEK GIHRLLDYDG IIEVDSGSFQ LMRYGKVEVT NREIVEFQHK
IGVDIGTFLD IPTPPDAPRE KAEQDLKITL ERAKEAESIK QIPMNATVQG STYLDLRKLA
ARKLSEMNFE IHPIGAVVPL LESYRFKDVV DIVIASKMGL RPDRPVHLFG AGHPMVFALA
VAMGVDLFDS ASYALYAKDD RYLTPQGTKR LEELEYFSCS CPVCSKYTPQ ELREMPKEER
EKLLALHNLW VIREEINRVK QAIKEGELWR LVDERARAHP KLYAAYKRLL EYYHYLEEYE
PITKKSAFFK ISEESLKWPI ARRAKERAEK VKAKFPESIP HPIFGEIPKY LSLTYPFAQS
ESEEDFQIEK PTRENAILYI MAIAEYQFGE GAGEAFRDAE VEIAKTGMPR QVKKNGKRLA
TVRAEDGLLT LGIEGAKRLH ELLPYPVMRV VVNKEAEPFA RKGKDVFAKF VEFADPKIRP
YDEVLIVNEN DELLATGQAL LSGREMVLFS SGRAVKTRRG VEEKK
