ID   DGTP_YERPG              Reviewed;         506 AA.
AC   A9R1D9;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Deoxyguanosinetriphosphate triphosphohydrolase {ECO:0000255|HAMAP-Rule:MF_00030};
DE            Short=dGTP triphosphohydrolase {ECO:0000255|HAMAP-Rule:MF_00030};
DE            Short=dGTPase {ECO:0000255|HAMAP-Rule:MF_00030};
DE            EC=3.1.5.1 {ECO:0000255|HAMAP-Rule:MF_00030};
GN   Name=dgt {ECO:0000255|HAMAP-Rule:MF_00030};
GN   OrderedLocusNames=YpAngola_A0988;
OS   Yersinia pestis bv. Antiqua (strain Angola).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=349746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Angola;
RX   PubMed=20061468; DOI=10.1128/jb.01518-09;
RA   Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S.,
RA   Achtman M., Lindler L.E., Ravel J.;
RT   "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals
RT   new insights into the evolution and pangenome of the plague bacterium.";
RL   J. Bacteriol. 192:1685-1699(2010).
CC   -!- FUNCTION: dGTPase preferentially hydrolyzes dGTP over the other
CC       canonical NTPs. {ECO:0000255|HAMAP-Rule:MF_00030}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dGTP + H2O = 2'-deoxyguanosine + H(+) + triphosphate;
CC         Xref=Rhea:RHEA:15193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17172, ChEBI:CHEBI:18036, ChEBI:CHEBI:61429; EC=3.1.5.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00030};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00030};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00030}.
CC   -!- SIMILARITY: Belongs to the dGTPase family. Type 1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00030}.
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DR   EMBL; CP000901; ABX85369.1; -; Genomic_DNA.
DR   RefSeq; WP_002209369.1; NZ_CP009935.1.
DR   AlphaFoldDB; A9R1D9; -.
DR   SMR; A9R1D9; -.
DR   GeneID; 57975326; -.
DR   KEGG; ypg:YpAngola_A0988; -.
DR   PATRIC; fig|349746.12.peg.1939; -.
DR   OMA; ICYTIID; -.
DR   GO; GO:0008832; F:dGTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006203; P:dGTP catabolic process; IEA:InterPro.
DR   CDD; cd00077; HDc; 1.
DR   Gene3D; 1.10.3410.10; -; 1.
DR   HAMAP; MF_00030; dGTPase_type1; 1.
DR   InterPro; IPR023293; dGTP_triP_hydro_central_sf.
DR   InterPro; IPR006261; dNTPase.
DR   InterPro; IPR020779; dNTPase_1.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR006674; HD_domain.
DR   InterPro; IPR026875; PHydrolase_assoc_dom.
DR   PANTHER; PTHR11373:SF32; PTHR11373:SF32; 1.
DR   Pfam; PF01966; HD; 1.
DR   Pfam; PF13286; HD_assoc; 1.
DR   SMART; SM00471; HDc; 1.
DR   TIGRFAMs; TIGR01353; dGTP_triPase; 1.
DR   PROSITE; PS51831; HD; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium.
FT   CHAIN           1..506
FT                   /note="Deoxyguanosinetriphosphate triphosphohydrolase"
FT                   /id="PRO_1000090268"
FT   DOMAIN          66..274
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ   SEQUENCE   506 AA;  58424 MW;  75BC0E14B179D4CA CRC64;
     MSGIDFKQKI SFQRPFSKPS SAEDEYEITR VFESDRGRIV NSAAIRRLQQ KTQVFPLERN
     AAVRSRLTHS LEVQQVGRYI AKEILNRFKQ DKKITAYGLD KLLDPFESIV EMACLMHDIG
     NPPFGHFGES AINDWFTKRM DPNGGSGSEP QSTDQCQVDV LKLCEGETEL NILRSKIRHD
     LSQFEGNAQA IRLVHSLLKL NLTYAQVGCI LKYTKPAYWS APIPASHNYL MKKPGFYLAE
     ENYVKELRRE LNMEEFDRFP LTYIMEAADD ISYCIADLED AVEKNIFSVE QLYDHMSQEW
     GAVTPGDLFD KVVGAAFRQL GREQGRRSSE DQFFMYLRVN TVGKLVPHAA QRFIENLPAV
     FSGSFNQALL EDSSAACKLL QIFKRVAVKH VFNHPEVEQL ELQGYRVISG LLDIYSPLLA
     MPETAFTQLV ADDRHRKYPI ETRLFHKLSI KHRLAYAESA ERIRNLPSEQ YEIYEYYYRA
     RLIQDYISGM TDLYAYDEYR RLMAAE