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Database: UniProt
Entry: A0A1I4YYG0_9RHOB
LinkDB: A0A1I4YYG0_9RHOB
Original site: A0A1I4YYG0_9RHOB 
ID   A0A1I4YYG0_9RHOB        Unreviewed;       132 AA.
AC   A0A1I4YYG0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=8-oxo-dGTP diphosphatase {ECO:0000256|ARBA:ARBA00040794};
DE            EC=3.6.1.55 {ECO:0000256|ARBA:ARBA00038905};
DE   AltName: Full=7,8-dihydro-8-oxoguanine-triphosphatase {ECO:0000256|ARBA:ARBA00042798};
DE   AltName: Full=Mutator protein MutT {ECO:0000256|ARBA:ARBA00041979};
DE   AltName: Full=dGTP pyrophosphohydrolase {ECO:0000256|ARBA:ARBA00041592};
GN   ORFNames=SAMN04487859_102149 {ECO:0000313|EMBL:SFN42823.1};
OS   Roseovarius lutimaris.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=1005928 {ECO:0000313|EMBL:SFN42823.1, ECO:0000313|Proteomes:UP000198599};
RN   [1] {ECO:0000313|EMBL:SFN42823.1, ECO:0000313|Proteomes:UP000198599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 28463 {ECO:0000313|EMBL:SFN42823.1,
RC   ECO:0000313|Proteomes:UP000198599};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=8-oxo-GTP + H2O = 8-oxo-GMP + diphosphate + H(+);
CC         Xref=Rhea:RHEA:67616, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:143553, ChEBI:CHEBI:145694;
CC         Evidence={ECO:0000256|ARBA:ARBA00036904};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=8-oxo-dGTP + H2O = 8-oxo-dGMP + diphosphate + H(+);
CC         Xref=Rhea:RHEA:31575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:63224, ChEBI:CHEBI:77896; EC=3.6.1.55;
CC         Evidence={ECO:0000256|ARBA:ARBA00035861};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|PIRSR:PIRSR603561-2};
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family.
CC       {ECO:0000256|ARBA:ARBA00005582}.
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DR   EMBL; FOVP01000002; SFN42823.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4YYG0; -.
DR   STRING; 1005928.SAMN04487859_102149; -.
DR   OrthoDB; 9810648at2; -.
DR   Proteomes; UP000198599; Unassembled WGS sequence.
DR   GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   CDD; cd03425; MutT_pyrophosphohydrolase; 1.
DR   Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR   InterPro; IPR003561; Mutator_MutT.
DR   InterPro; IPR047127; MutT-like.
DR   InterPro; IPR029119; MutY_C.
DR   InterPro; IPR020476; Nudix_hydrolase.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR020084; NUDIX_hydrolase_CS.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   NCBIfam; TIGR00586; mutt; 1.
DR   PANTHER; PTHR47707; 8-OXO-DGTP DIPHOSPHATASE; 1.
DR   PANTHER; PTHR47707:SF1; NUDIX HYDROLASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF14815; NUDIX_4; 1.
DR   PRINTS; PR00502; NUDIXFAMILY.
DR   SUPFAM; SSF55811; Nudix; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR603561-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR603561-2};
KW   Mutator protein {ECO:0000256|ARBA:ARBA00022457}.
FT   DOMAIN          1..130
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS51462"
FT   BINDING         23
FT                   /ligand="8-oxo-dGTP"
FT                   /ligand_id="ChEBI:CHEBI:77896"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603561-1"
FT   BINDING         34..37
FT                   /ligand="8-oxo-dGTP"
FT                   /ligand_id="ChEBI:CHEBI:77896"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603561-1"
FT   BINDING         37
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603561-2"
FT   BINDING         57
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603561-2"
SQ   SEQUENCE   132 AA;  14692 MW;  146DA99F368CE17B CRC64;
     MKIVLVSAVA LIDVDGRVLL AQRPVGKSMA GLWEFPGGKV EPGETPEHAL IRELQEELGI
     NTWSSCLAPL TFASHSYDDF HLLMPLFACR KWEGTAQGRE GQTLKWVRAA DLKSYPMPPA
     DIPLIPILRD WL
//
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