ID   DGTP_SHIB3              Reviewed;         505 AA.
AC   B2U304;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 76.
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=SbBS512_E0152;
OS   Shigella boydii serotype 18 (strain CDC 3083-94 / BS512).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=344609;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 3083-94 / BS512;
RA   Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R.,
RA   Jiang L., Ravel J., Sebastian Y.;
RT   "Complete sequence of Shigella boydii serotype 18 strain BS512.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001063; ACD09404.1; -; Genomic_DNA.
DR   RefSeq; WP_000057110.1; NC_010658.1.
DR   AlphaFoldDB; B2U304; -.
DR   SMR; B2U304; -.
DR   STRING; 344609.SbBS512_E0152; -.
DR   EnsemblBacteria; ACD09404; ACD09404; SbBS512_E0152.
DR   KEGG; sbc:SbBS512_E0152; -.
DR   HOGENOM; CLU_028163_2_1_6; -.
DR   OMA; ICYTIID; -.
DR   Proteomes; UP000001030; Chromosome.
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   PANTHER; PTHR11373:SF32; PTHR11373:SF32; 1.
DR   Pfam; PF01966; HD; 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..505
FT                   /note="Deoxyguanosinetriphosphate triphosphohydrolase"
FT                   /id="PRO_1000090266"
FT   DOMAIN          66..273
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ   SEQUENCE   505 AA;  59449 MW;  FDEDBAC6E8C78A6E CRC64;
     MAQIDFRKKI NWHRRYRSPQ GVKTEHEILR IFESDRGRII NSPAIRRLQQ KTQVFPLERN
     AAVRTRLTHS MEVQQVGRYI AKEILSRMKE LKLLEAYGLD ELTGPFESIV EMSCLMHDIG
     NPPFGHFGEA AINDWFRQRL HPEDAESQPL TDDRCSVAAL RLRDGEEPLN ELRRKIRQDL
     CHFEGNAQGI RLVHTLMRMN LTWAQVGGIL KYTRPAWWRG ETPETHHYLM KKPGYYLSEE
     AYIARLRKEL NLALYSRFPL TWIMEAADDI SYCVADLEDA VEKRIFTVEQ LYHHLHEAWG
     QHEKGSLFSL VVENAWEKSR SNSLSRSTED QFFMYLRVNT LNKLVPYAAQ RFIDNLPAIF
     AGTFNHALLE DASECSDLLK LYKNVAVKHV FSHPDVEQLE LQGYRVISGL LEIYRPLLSL
     SLSDFTELVE KERVKRFPIE SRLFHKLSTR HRLAYVEAVS KLPSDYPEFP LWEYYYRCRL
     LQDYISGMTD LYAWDEYRRL MAVEQ