ID A0A1U7GQG1_9BACT Unreviewed; 132 AA.
AC A0A1U7GQG1;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=8-oxo-dGTP diphosphatase {ECO:0000256|ARBA:ARBA00038905};
DE EC=3.6.1.55 {ECO:0000256|ARBA:ARBA00038905};
GN ORFNames=BGO49_06565 {ECO:0000313|EMBL:OJW24696.1};
OS Planctomycetales bacterium 71-10.
OC Bacteria; Planctomycetota; Planctomycetia; Planctomycetales.
OX NCBI_TaxID=1895807 {ECO:0000313|EMBL:OJW24696.1, ECO:0000313|Proteomes:UP000185848};
RN [1] {ECO:0000313|EMBL:OJW24696.1, ECO:0000313|Proteomes:UP000185848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=71-10 {ECO:0000313|EMBL:OJW24696.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the Nudix hydrolase family.
CC {ECO:0000256|ARBA:ARBA00005582}.
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:OJW24696.1}.
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DR EMBL; MKTT01000036; OJW24696.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U7GQG1; -.
DR STRING; 1895807.BGO49_06565; -.
DR Proteomes; UP000185848; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; 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 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};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Mutator protein {ECO:0000256|ARBA:ARBA00022457}.
FT DOMAIN 4..131
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 132 AA; 14379 MW; 17E624BDC16C6264 CRC64;
MPGDKLTLVG IGIIRRVSDG RYLIRERPAG TVYAGYWEFP GGKVEPGETP GQTTARECLE
ETGLAVSADR LRAVVEHTYP HGRVRLHFFD CTPIDPAANP DPACRWVAAA ELADYRFPEA
NEGILAELAA EG
//
