ATGT_PYRHO
ID ATGT_PYRHO Reviewed; 582 AA.
AC O58843;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=tRNA-guanine(15) transglycosylase;
DE EC=2.4.2.48;
DE AltName: Full=7-cyano-7-deazaguanine tRNA-ribosyltransferase;
DE AltName: Full=Archaeal tRNA-guanine transglycosylase;
GN Name=tgtA; OrderedLocusNames=PH1116;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG AND
RP ZINC ION, FUNCTION, COFACTOR, SUBUNIT, MUTAGENESIS OF ASP-95 AND SER-96,
RP AND ACTIVE SITE.
RX PubMed=12054814; DOI=10.1016/s0022-2836(02)00090-6;
RA Ishitani R., Nureki O., Fukai S., Kijimoto T., Nameki N., Watanabe M.,
RA Kondo H., Sekine M., Okada N., Nishimura S., Yokoyama S.;
RT "Crystal structure of archaeosine tRNA-guanine transglycosylase.";
RL J. Mol. Biol. 318:665-677(2002).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) IN COMPLEX WITH ZINC ION, COFACTOR,
RP AND SUBUNIT.
RX PubMed=12732145; DOI=10.1016/s0092-8674(03)00280-0;
RA Ishitani R., Nureki O., Nameki N., Okada N., Nishimura S., Yokoyama S.;
RT "Alternative tertiary structure of tRNA for recognition by a
RT posttranscriptional modification enzyme.";
RL Cell 113:383-394(2003).
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:12054814}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:12054814, ECO:0000269|PubMed:12732145};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:12054814,
CC ECO:0000269|PubMed:12732145};
CC -!- PATHWAY: tRNA modification; archaeosine-tRNA biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12054814,
CC ECO:0000269|PubMed:12732145}.
CC -!- SIMILARITY: Belongs to the archaeosine tRNA-ribosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; BA000001; BAA30215.1; -; Genomic_DNA.
DR PIR; E71052; E71052.
DR RefSeq; WP_010885200.1; NC_000961.1.
DR PDB; 1IQ8; X-ray; 2.20 A; A/B=1-582.
DR PDB; 1IT7; X-ray; 2.30 A; A/B=1-582.
DR PDB; 1IT8; X-ray; 2.50 A; A/B=1-582.
DR PDB; 1J2B; X-ray; 3.30 A; A/B=1-582.
DR PDBsum; 1IQ8; -.
DR PDBsum; 1IT7; -.
DR PDBsum; 1IT8; -.
DR PDBsum; 1J2B; -.
DR AlphaFoldDB; O58843; -.
DR SMR; O58843; -.
DR STRING; 70601.3257532; -.
DR EnsemblBacteria; BAA30215; BAA30215; BAA30215.
DR GeneID; 1443435; -.
DR KEGG; pho:PH1116; -.
DR eggNOG; arCOG00989; Archaea.
DR eggNOG; arCOG00991; Archaea.
DR OMA; FPCSCPV; -.
DR OrthoDB; 10236at2157; -.
DR BRENDA; 2.4.2.48; 5244.
DR UniPathway; UPA00393; -.
DR EvolutionaryTrace; O58843; -.
DR Proteomes; UP000000752; 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 3D-structure; Glycosyltransferase; Metal-binding; Transferase;
KW tRNA processing; Zinc.
FT CHAIN 1..582
FT /note="tRNA-guanine(15) transglycosylase"
FT /id="PRO_0000247617"
FT DOMAIN 507..582
FT /note="PUA"
FT ACT_SITE 95
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:12054814"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12054814"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12054814"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:12054814,
FT ECO:0000269|PubMed:12732145"
FT BINDING 281
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:12054814,
FT ECO:0000269|PubMed:12732145"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:12054814,
FT ECO:0000269|PubMed:12732145"
FT MUTAGEN 95
FT /note="D->A: Abolishes the transferase activity."
FT /evidence="ECO:0000269|PubMed:12054814"
FT MUTAGEN 96
FT /note="S->A: Weak decrease in transferase activity."
FT /evidence="ECO:0000269|PubMed:12054814"
FT STRAND 8..16
FT /evidence="ECO:0007829|PDB:1IQ8"
FT STRAND 19..26
FT /evidence="ECO:0007829|PDB:1IQ8"
FT STRAND 29..39
FT /evidence="ECO:0007829|PDB:1IQ8"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1IQ8"
FT HELIX 49..54
FT /evidence="ECO:0007829|PDB:1IQ8"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:1IQ8"
FT HELIX 64..69
FT /evidence="ECO:0007829|PDB:1IQ8"
FT HELIX 71..86
FT /evidence="ECO:0007829|PDB:1IQ8"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:1IQ8"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:1IQ8"
FT HELIX 111..120
FT /evidence="ECO:0007829|PDB:1IQ8"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:1IQ8"
FT HELIX 139..159
FT /evidence="ECO:0007829|PDB:1IQ8"
FT HELIX 174..186
FT /evidence="ECO:0007829|PDB:1IQ8"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:1IQ8"
FT HELIX 198..202
FT /evidence="ECO:0007829|PDB:1IQ8"
FT HELIX 206..219
FT /evidence="ECO:0007829|PDB:1IQ8"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:1IQ8"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:1IQ8"
FT HELIX 237..242
FT /evidence="ECO:0007829|PDB:1IQ8"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:1IQ8"
FT HELIX 252..258
FT /evidence="ECO:0007829|PDB:1IQ8"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:1IQ8"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:1IQ8"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:1IQ8"
FT TURN 282..286
FT /evidence="ECO:0007829|PDB:1IQ8"
FT HELIX 289..292
FT /evidence="ECO:0007829|PDB:1IQ8"
FT HELIX 297..325
FT /evidence="ECO:0007829|PDB:1IQ8"
FT HELIX 328..336
FT /evidence="ECO:0007829|PDB:1IQ8"
FT HELIX 340..351
FT /evidence="ECO:0007829|PDB:1IQ8"
FT HELIX 353..359
FT /evidence="ECO:0007829|PDB:1IQ8"
FT HELIX 374..377
FT /evidence="ECO:0007829|PDB:1IQ8"
FT HELIX 379..395
FT /evidence="ECO:0007829|PDB:1IQ8"
FT STRAND 398..401
FT /evidence="ECO:0007829|PDB:1IQ8"
FT TURN 402..404
FT /evidence="ECO:0007829|PDB:1IQ8"
FT STRAND 405..408
FT /evidence="ECO:0007829|PDB:1IQ8"
FT HELIX 409..411
FT /evidence="ECO:0007829|PDB:1IQ8"
FT TURN 415..417
FT /evidence="ECO:0007829|PDB:1IQ8"
FT STRAND 418..421
FT /evidence="ECO:0007829|PDB:1IQ8"
FT TURN 433..435
FT /evidence="ECO:0007829|PDB:1IQ8"
FT HELIX 436..448
FT /evidence="ECO:0007829|PDB:1IQ8"
FT HELIX 452..455
FT /evidence="ECO:0007829|PDB:1IQ8"
FT TURN 456..458
FT /evidence="ECO:0007829|PDB:1IQ8"
FT STRAND 460..463
FT /evidence="ECO:0007829|PDB:1IQ8"
FT STRAND 465..467
FT /evidence="ECO:0007829|PDB:1IQ8"
FT STRAND 469..473
FT /evidence="ECO:0007829|PDB:1IQ8"
FT STRAND 475..482
FT /evidence="ECO:0007829|PDB:1IQ8"
FT TURN 484..486
FT /evidence="ECO:0007829|PDB:1IQ8"
FT STRAND 489..491
FT /evidence="ECO:0007829|PDB:1IQ8"
FT HELIX 493..502
FT /evidence="ECO:0007829|PDB:1IQ8"
FT TURN 505..508
FT /evidence="ECO:0007829|PDB:1IQ8"
FT STRAND 509..512
FT /evidence="ECO:0007829|PDB:1IQ8"
FT TURN 514..516
FT /evidence="ECO:0007829|PDB:1IQ8"
FT HELIX 517..521
FT /evidence="ECO:0007829|PDB:1IQ8"
FT HELIX 528..530
FT /evidence="ECO:0007829|PDB:1IQ8"
FT STRAND 531..534
FT /evidence="ECO:0007829|PDB:1IQ8"
FT STRAND 543..547
FT /evidence="ECO:0007829|PDB:1IQ8"
FT STRAND 553..561
FT /evidence="ECO:0007829|PDB:1IQ8"
FT HELIX 563..568
FT /evidence="ECO:0007829|PDB:1IQ8"
FT STRAND 571..580
FT /evidence="ECO:0007829|PDB:1IQ8"
SQ SEQUENCE 582 AA; 66596 MW; B96F1D5EC0D73AC3 CRC64;
MSRGDKMLKF EIKARDGAGR IGKLEVNGKK IETPAIMPVV NPKQMVVEPK ELEKMGFEII
ITNSYIIYKD EELRRKALEL GIHRMLDYNG IIEVDSGSFQ LMKYGSIEVS NREIIEFQHR
IGVDIGTFLD IPTPPDAPRE QAVKELEITL SRAREAEEIK EIPMNATIQG STYTDLRRYA
ARRLSSMNFE IHPIGGVVPL LESYRFRDVV DIVISSKMAL RPDRPVHLFG AGHPIVFALA
VAMGVDLFDS ASYALYAKDD RYMTPEGTKR LDELDYFPCS CPVCSKYTPQ ELREMPKEER
TRLLALHNLW VIKEEIKRVK QAIKEGELWR LVDERARSHP KLYSAYKRLL EHYTFLEEFE
PITKKSALFK ISNESLRWPV VRRAKERAKS INERFGELVE HPIFGRVSRY LSLTYPFAQS
EAEDDFKIEK PTKEDAIKYV MAIAEYQFGE GASRAFDDAK VELSKTGMPR QVKVNGKRLA
TVRADDGLLT LGIEGAKRLH RVLPYPRMRV VVNKEAEPFA RKGKDVFAKF VIFADPGIRP
YDEVLVVNEN DELLATGQAL LSGREMIVFQ YGRAVKVRKG VE
