ID   DGTP_KLEP7              Reviewed;         504 AA.
AC   A6T4W4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, 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=KPN78578_01740; ORFNames=KPN_00175;
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=272620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578;
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-2006) 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; CP000647; ABR75635.1; -; Genomic_DNA.
DR   RefSeq; WP_004145871.1; NC_009648.1.
DR   AlphaFoldDB; A6T4W4; -.
DR   SMR; A6T4W4; -.
DR   STRING; 272620.KPN_00175; -.
DR   EnsemblBacteria; ABR75635; ABR75635; KPN_00175.
DR   KEGG; kpn:KPN_00175; -.
DR   HOGENOM; CLU_028163_2_1_6; -.
DR   OMA; ICYTIID; -.
DR   Proteomes; UP000000265; 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; Reference proteome.
FT   CHAIN           1..504
FT                   /note="Deoxyguanosinetriphosphate triphosphohydrolase"
FT                   /id="PRO_1000006549"
FT   DOMAIN          66..273
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ   SEQUENCE   504 AA;  59004 MW;  7A1F5A3214A06C2A CRC64;
     MAKIDFRNKI NWRRRFRSPP RVETERDILR IFESDRGRIV NSPAIRRLQQ KTQVFPLERN
     AAVRTRLTHS LEVQQVGRYI AKEVLSRLKE LRLLEEYGLE ELTGPFESVV EMACLMHDIG
     NPPFGHFGEA AINDWFRQRL APGDALGQPL TDDRCEVQAL RLHDGETSLN ALRRKVRQDL
     CSFEGNAQGI RLVHTLMRMN LTWAQVGCIL KYTRPAWWSE ETPASHSYLM KKPGYYLAEE
     EYVARLRKEL DLAPYNRFPL TWIMEAADDI SYCVADLEDA VEKRIFSAEQ LYQHLYDAWG
     SHEKGSLFSQ VVENAWEKSR ANYLKQSAED QFFMYLRVNT LNKLVPYAAR RFIDNLPAIF
     TGDFNHALLE DDSDCSQLLE LYKNVAMKQV FSHPDVEQLE LQGYRVISGL LDIYQPLLKL
     SLEDFSELVA QERVRRLPIA SRLYQKLSTR HRLAYVEAVN KLARTAPEFA LMEYYYRCRL
     IQDYISGMTD LYAWDEYRRL MAVE