ID   DGTP_SALPA              Reviewed;         505 AA.
AC   Q5PD54;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=SPA0214;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV76244.1; -; Genomic_DNA.
DR   RefSeq; WP_000146453.1; NC_006511.1.
DR   AlphaFoldDB; Q5PD54; -.
DR   SMR; Q5PD54; -.
DR   EnsemblBacteria; AAV76244; AAV76244; SPA0214.
DR   KEGG; spt:SPA0214; -.
DR   HOGENOM; CLU_028163_2_1_6; -.
DR   OMA; ICYTIID; -.
DR   Proteomes; UP000008185; 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   CHAIN           1..505
FT                   /note="Deoxyguanosinetriphosphate triphosphohydrolase"
FT                   /id="PRO_1000006551"
FT   DOMAIN          66..273
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ   SEQUENCE   505 AA;  59509 MW;  4B51CD9AB8BEE3B7 CRC64;
     MASIDFRNKI NWHRRYRSPQ GVKTEHEILR IFESDRGRII NSPAIRRLQQ KTQVFPLERN
     AAVRTRLTHS MEVQQVGRYI AKEILSRLKE QNRLEEYGLD ALTGPFESIV EMACLMHDIG
     NPPFGHFGEA AINDWFRQWL HPEDAESQPL THDRCVVSSL RLQEGEENLN DIRRKVRQDI
     CHFEGNAQGI RLVHTLMRMN LTWAQVGGIL KYTRPAWWRG PVPDSHRYLM KKPGYYLSEE
     KYIARLRKEL QLAPYSRFPL TWIMEAADDI SYCVADLEDA VEKRIFSVEQ LYHHLYHAWG
     HHEKDSLFEL VVGNAWEKSR ANTLSRSTED QFFMYLRVNT LNKLVSYAAQ RFIDNLPQIF
     AGTFNQALLE DASGFSRLLE LYKNVAVEHV FSHPDVEQLE LQGYRVISGL LDIYQPLLSL
     SLNDFRELVE KERLKRFPIE SRLFQKLSTR HRLAYVEVVS KLPTDSAEYP VLEYYYRCRL
     IQDYISGMTD LYAWDEYRRL MAVEQ