ID   DGTP_ECOL6              Reviewed;         505 AA.
AC   Q8FL13;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 106.
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}; OrderedLocusNames=c0196;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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; AE014075; AAN78690.1; -; Genomic_DNA.
DR   RefSeq; WP_000057086.1; NC_004431.1.
DR   AlphaFoldDB; Q8FL13; -.
DR   SMR; Q8FL13; -.
DR   STRING; 199310.c0196; -.
DR   PRIDE; Q8FL13; -.
DR   EnsemblBacteria; AAN78690; AAN78690; c0196.
DR   KEGG; ecc:c0196; -.
DR   eggNOG; COG0232; Bacteria.
DR   HOGENOM; CLU_028163_2_1_6; -.
DR   OMA; ICYTIID; -.
DR   BioCyc; ECOL199310:C0196-MON; -.
DR   Proteomes; UP000001410; 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   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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..505
FT                   /note="Deoxyguanosinetriphosphate triphosphohydrolase"
FT                   /id="PRO_0000205280"
FT   DOMAIN          66..273
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ   SEQUENCE   505 AA;  59374 MW;  C2488EDEC086129E CRC64;
     MAQIDFRKKI NWHRRYRSPQ GVKTEHEILR IFESDRGRII NSPAIRRLQQ KTQVFPLERN
     AAVRTRLTHS MEVQQVGRYI AKEILSRLKE LKLLEAYGLD ELTGPFESIV EMSCLMHDIG
     NPPFGHFGEA AINDWFRQRL YPEDAESQPL TDDRCSVAAL RLRDGEEPLN ALRRKIRQDL
     CHFEGNAQGI RLVHTLMRMN LTWAQVGGIL KYTRPAWWRG ETPETHHYLM KKPGYYLSEE
     AYIARLRKEL NLALYSRFPL TWIMEAADDI SYCVADLEDA VEKRIFTVEQ LYHHLHEAWG
     QHEKGSLFSL VVENAWEKSR SNSLSRSTED QFFMYLRVNT LNKLVPYAAQ RFIDNLPAIF
     AGTFNHALLE DASECSDLLK LYKNVAVKHV FSHPDVEQLE LQGYRVISGL LEIYRPLLNL
     PLSDFTELVE KERVKRFPIE TRLFHKLSTR HRLAYVEAVS KLPSDSPEFP LWEYYYRCRL
     LQDYISGMTD LYAWDEYRRL MAVEQ