ATGT_PYRAB
ID ATGT_PYRAB Reviewed; 584 AA.
AC Q9UZN0; G8ZJS1;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=PYRAB11160;
GN ORFNames=PAB0740;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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; AJ248286; CAB50027.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70530.1; -; Genomic_DNA.
DR PIR; F75090; F75090.
DR RefSeq; WP_010868234.1; NC_000868.1.
DR AlphaFoldDB; Q9UZN0; -.
DR SMR; Q9UZN0; -.
DR STRING; 272844.PAB0740; -.
DR EnsemblBacteria; CAB50027; CAB50027; PAB0740.
DR GeneID; 1496475; -.
DR KEGG; pab:PAB0740; -.
DR PATRIC; fig|272844.11.peg.1173; -.
DR eggNOG; arCOG00989; Archaea.
DR eggNOG; arCOG00991; Archaea.
DR HOGENOM; CLU_030083_0_0_2; -.
DR OMA; FPCSCPV; -.
DR OrthoDB; 10236at2157; -.
DR PhylomeDB; Q9UZN0; -.
DR UniPathway; UPA00393; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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 3: Inferred from homology;
KW Glycosyltransferase; Metal-binding; Transferase; tRNA processing; Zinc.
FT CHAIN 1..584
FT /note="tRNA-guanine(15) transglycosylase"
FT /id="PRO_0000247882"
FT DOMAIN 507..582
FT /note="PUA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
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 584 AA; 66668 MW; E31755EAE3681666 CRC64;
MSRGDKMLKF EVKARDGAGR IGKLEVNGKK IETPAIMPVV NPKQLIVEPK ELEKMGFDII
ITNSYIIYKD RELREKALEV GIHKLLGYDG IIEVDSGSFQ LMRYGNVDVS NREIVEFQHR
IGVDIGTFLD IPTPPDAPKE KAMEDLKITL ERAREAEEIK EIAMNAAIQG STYTDLRRYA
ARRLSSMNFE IHPIGGVVPL LEAYRFREVV DIVISSKMAL RPDRPVHLFG AGHPMVFALA
VAMGVDLFDS ASYALYAKDD RYLTPEGTKR LDELEYFPCS CPVCSRYTPQ ELREMPKEER
ARLLAIHNLW VIKEEIERIK QAIREGELWR LVDERARSHP KLYSAYKRLL DHYTFLEEFE
PVTKKSAVFK ISHESLRWPL VRRARERAER VNSKFGDLVE HPIFGKVTKY LTLTYPFAQS
EAEDEFSIEK PTRENAIRYV MAIAEYQFGE NASKAFEGAE VELARTGMPR QVKLNGKRLA
TVRAEDGFLT LGIEGAKRLH KVLEYPRMRV VVSEEAEPFA RKGKDVFAKF VLFADPGIRP
YDEVLVVNEK DELLATGQAL MSGREMIVFQ YGRAVKVRRG ISGG
