ID   A0A078LNV7_9PSED        Unreviewed;       498 AA.
AC   A0A078LNV7;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Probable deoxyguanosinetriphosphate triphosphohydrolase {ECO:0000256|HAMAP-Rule:MF_00030};
DE            Short=dGTP triphosphohydrolase {ECO:0000256|HAMAP-Rule:MF_00030};
DE            Short=dGTPase {ECO:0000256|HAMAP-Rule:MF_00030};
DE            EC=3.1.5.1 {ECO:0000256|HAMAP-Rule:MF_00030};
GN   Name=dgt {ECO:0000256|HAMAP-Rule:MF_00030,
GN   ECO:0000313|EMBL:CDZ92799.1};
GN   ORFNames=BN1079_00068 {ECO:0000313|EMBL:CDZ92799.1};
OS   Pseudomonas saudiphocaensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1499686 {ECO:0000313|EMBL:CDZ92799.1, ECO:0000313|Proteomes:UP000053902};
RN   [1] {ECO:0000313|EMBL:CDZ92799.1, ECO:0000313|Proteomes:UP000053902}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=20_BN {ECO:0000313|EMBL:CDZ92799.1,
RC   ECO:0000313|Proteomes:UP000053902};
RA   Urmite Genomes Urmite Genomes;
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: dGTPase preferentially hydrolyzes dGTP over the other
CC       canonical NTPs. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00030};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00030};
CC   -!- SIMILARITY: Belongs to the dGTPase family. Type 1 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00030}.
CC   -!- CAUTION: As this bacterium is not an Enterobacterale, this protein may
CC       not have a true dGTPase activity. {ECO:0000256|HAMAP-Rule:MF_00030}.
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DR   EMBL; CCSF01000001; CDZ92799.1; -; Genomic_DNA.
DR   RefSeq; WP_037021510.1; NZ_CCSF01000001.1.
DR   AlphaFoldDB; A0A078LNV7; -.
DR   STRING; 1499686.BN1079_00068; -.
DR   eggNOG; COG0232; Bacteria.
DR   HOGENOM; CLU_028163_2_1_6; -.
DR   OrthoDB; 9803619at2; -.
DR   Proteomes; UP000053902; Unassembled WGS sequence.
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; 1.10.3210.10; Hypothetical protein af1432; 1.
DR   Gene3D; 1.10.3410.10; putative deoxyguanosinetriphosphate triphosphohydrolase like domain; 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   NCBIfam; TIGR01353; dGTP_triPase; 1.
DR   PANTHER; PTHR11373:SF32; DEOXYGUANOSINETRIPHOSPHATE TRIPHOSPHOHYDROLASE; 1.
DR   PANTHER; PTHR11373; DEOXYNUCLEOSIDE TRIPHOSPHATE TRIPHOSPHOHYDROLASE; 1.
DR   SMART; SM00471; HDc; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   PROSITE; PS51831; HD; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00030, ECO:0000313|EMBL:CDZ92799.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00030};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053902}.
FT   DOMAIN          72..263
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
SQ   SEQUENCE   498 AA;  56378 MW;  D1D9FE63D30D7D40 CRC64;
     MPMPVNFKNK ISRQRPYGRL EEGLKPSECD LSLIVDQLES DRGRIINSAG VRRLQQKTQV
     FPLERNAAVR SRLTHSLEVQ QTGRFIVRTL YRQLGEKAPI YGLDGLEGVL ESLVEMTCLM
     HDTGNPPFGH FGEFSIGQWF GRHLEELFEA AVPHGRGDES LRTRMLADLR AFEGNAQAIR
     LVVSLQRLNL TYAQTAGLLK YVRPAYMPKP EKGSPGAYLH KKPGYYLSEE RFVADLQAAL
     GLAPGTRHPV AYVMEAADDI AYCLADIEDS VEKGIFSIEQ LAGLLVEKFA EHGSPDEPIG
     ATGRSFRSMV AYAESRAQRE TINKVGEFFI WLRVNLVHPL VQHAARQFIE HIEAVYHGTL
     DRALLEDASL ENAIVQTFKD VAMEHVFCHR EVETLQLQGY RILQGLLDFY APLLRVPVPV
     FHELTEGVCR SEPHLQMLAR RLPSQLIKAY HEALTEHAES APDYPLWAFY YRCRMLQDFV
     SGMTDQLAQD EFRTLSAL
//