ID B7RSP9_9GAMM Unreviewed; 131 AA.
AC B7RSP9;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 58.
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=GPB2148_3062 {ECO:0000313|EMBL:EEB80248.1};
OS marine gamma proteobacterium HTCC2148.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae.
OX NCBI_TaxID=247634 {ECO:0000313|EMBL:EEB80248.1, ECO:0000313|Proteomes:UP000002793};
RN [1] {ECO:0000313|Proteomes:UP000002793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2148 {ECO:0000313|Proteomes:UP000002793};
RX PubMed=20472793; DOI=10.1128/jb.00511-10;
RA Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA Giovannoni S.J.;
RT "Genome sequences of strains HTCC2148 and HTCC2080, belonging to the
RT OM60/NOR5 clade of the Gammaproteobacteria.";
RL J. Bacteriol. 192:3842-3843(2010).
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; DS999222; EEB80248.1; -; Genomic_DNA.
DR AlphaFoldDB; B7RSP9; -.
DR STRING; 247634.GPB2148_3062; -.
DR eggNOG; COG0494; Bacteria.
DR HOGENOM; CLU_037162_19_2_6; -.
DR OrthoDB; 9810648at2; -.
DR Proteomes; UP000002793; 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:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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; 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.
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, ECO:0000313|EMBL:EEB80248.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR603561-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR603561-2};
KW Mutator protein {ECO:0000256|ARBA:ARBA00022457};
KW Reference proteome {ECO:0000313|Proteomes:UP000002793}.
FT DOMAIN 3..129
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 28
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"
FT BINDING 119
FT /ligand="8-oxo-dGTP"
FT /ligand_id="ChEBI:CHEBI:77896"
FT /evidence="ECO:0000256|PIRSR:PIRSR603561-1"
SQ SEQUENCE 131 AA; 14508 MW; 2F07135BBD3B1F15 CRC64;
MQVVHVAVGV ILDAEKNILL TRRHDHLHQG GLWEFPGGKV EQGESLDAAL ARELHEELAI
KPVKTSPLIE IHHDYPDKSV FLDVHVVWEY SGEAQGVEGQ PMAWVSAAEL SDYDFPEANK
PIVAAIVLEL T
//
