ID   DGTP_PSEAE              Reviewed;         498 AA.
AC   Q9I4L1;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Probable 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=PA1124;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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   -!- SIMILARITY: Belongs to the dGTPase family. Type 1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00030}.
CC   -!- CAUTION: As this bacterium is not an Enterobacteriaceae, this protein
CC       may not have a true dGTPase activity. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE004091; AAG04513.1; -; Genomic_DNA.
DR   PIR; H83505; H83505.
DR   RefSeq; NP_249815.1; NC_002516.2.
DR   RefSeq; WP_003112492.1; NZ_QZGE01000006.1.
DR   AlphaFoldDB; Q9I4L1; -.
DR   SMR; Q9I4L1; -.
DR   STRING; 287.DR97_810; -.
DR   PaxDb; Q9I4L1; -.
DR   PRIDE; Q9I4L1; -.
DR   EnsemblBacteria; AAG04513; AAG04513; PA1124.
DR   GeneID; 880761; -.
DR   KEGG; pae:PA1124; -.
DR   PATRIC; fig|208964.12.peg.1169; -.
DR   PseudoCAP; PA1124; -.
DR   HOGENOM; CLU_028163_2_1_6; -.
DR   InParanoid; Q9I4L1; -.
DR   OMA; ICYTIID; -.
DR   PhylomeDB; Q9I4L1; -.
DR   BioCyc; PAER208964:G1FZ6-1150-MON; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0008832; F:dGTPase activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006203; P:dGTP catabolic process; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..498
FT                   /note="Probable deoxyguanosinetriphosphate
FT                   triphosphohydrolase"
FT                   /id="PRO_0000205283"
FT   DOMAIN          71..262
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ   SEQUENCE   498 AA;  56742 MW;  939D09998A9A35E6 CRC64;
     MPGAVDFKER ISRQRPHDRE TYGHAGNTDL QDIVYQLESD RGRIVNSAAV RRLQQKTQVF
     PLERNAAVRS RLTHSLEVQQ TGRFIVRTLF RQLGPRAAEV GLDGLEGALE SLVEMACLMH
     DVGNPPFGHF GEYAINDWFE RNLDALFERR IPPGQGDGLL QQRMLTDLKH FEGNAQAIRL
     VVKLLRLNLT YTQTAGLLKY VRPAYEPKPD KAAANHYLNK KPGFYLSEEA FVDELRRVLG
     MRPGTRHPVA YIMEAADDIS YCLADIEDSV EKGILDIRQL ADLLVKKFAV HHSPDAPIPG
     DADNMSFQRM VDYSLEKAER EPINKVSEFF IRLRVKMIHP LVQHAAQQFI DNFEAVHAGT
     LGRALMEDGS LPHAIVQTFK DVAMEWVFCH PEVETLELQG YRIIQGLLDF YAPLLRLPAE
     EFQALAEGRQ AAAPHPQLLV RRLPSQQIKA YLEAMKGVAE DPLQRQWEFY HRCRMLQDFV
     SGMTDQHAQD EYRALSAL