ID A0A1S8CIM4_9GAMM Unreviewed; 505 AA.
AC A0A1S8CIM4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=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 ORFNames=BMI79_12310 {ECO:0000313|EMBL:OMQ22292.1};
OS Serratia oryzae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=2034155 {ECO:0000313|EMBL:OMQ22292.1, ECO:0000313|Proteomes:UP000216021};
RN [1] {ECO:0000313|EMBL:OMQ22292.1, ECO:0000313|Proteomes:UP000216021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J11-6 {ECO:0000313|EMBL:OMQ22292.1,
RC ECO:0000313|Proteomes:UP000216021};
RA Zhang X.-X., Zhang J.;
RT "Rahnella oryzae sp. nov., isolated from rice root.";
RL Submitted (NOV-2016) 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 -!- SUBUNIT: Homotetramer. {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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OMQ22292.1}.
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DR EMBL; MOXD01000006; OMQ22292.1; -; Genomic_DNA.
DR RefSeq; WP_076942499.1; NZ_MOXD01000006.1.
DR AlphaFoldDB; A0A1S8CIM4; -.
DR STRING; 2034155.BMI79_12310; -.
DR OrthoDB; 9803619at2; -.
DR Proteomes; UP000216021; 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; 2.
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 InterPro; IPR026875; PHydrolase_assoc_dom.
DR NCBIfam; TIGR01353; dGTP_triPase; 1.
DR PANTHER; PTHR11373:SF32; DEOXYGUANOSINETRIPHOSPHATE TRIPHOSPHOHYDROLASE; 1.
DR PANTHER; PTHR11373; DEOXYNUCLEOSIDE TRIPHOSPHATE TRIPHOSPHOHYDROLASE; 1.
DR Pfam; PF01966; HD; 1.
DR Pfam; PF13286; HD_assoc; 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};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00030}.
FT DOMAIN 66..273
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
SQ SEQUENCE 505 AA; 58476 MW; 66B51C22FD5B53BB CRC64;
MSGIDFKQKI SFQRPFSKPV EAEEEYDIVR QFESDRGRIV NSAAIRRLQQ KTQVFPLERN
AAVRSRLTHS MEVQQVGRHI AKEILNRFKQ DQRIDALGLS KLLDPFESIV EMACLMHDIG
NPPFGHFGES AINNWFRQRL DPANCGSEPS SHEGCSVDVL RLREGESDLN RLRSRIREDL
SQFEGNAQAI RLVHTLLKLN LTYAQVGCIL KYTRPAYWAS DIPDSHSYLM KKPGFYLAEE
AFVDRLRREL NMGEFDRFPL TYIMEAADDI SYCVADLEDA VEKNIFTVEQ LYQHLTQEWG
EVTPGDLFDK TVASAFRKID RGGARRSSED QFFMYLRVFT VARLVPHAAQ RFIDNLDAVF
HGRFNGALLE DTSPVYKLLE IFKNVAFKHV FNHPEVEQLE LQGYRVISGL LDIYSPLLAM
SQADFSQLVR DDSHRAFPIE TRLFHKLSTK HRLAYVEAVE GLQHLSTEQQ AIREYYFRAR
LLQDYISGMT DLYAYDEYRR LMAAE
//
