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Database: UniProt
Entry: A0A1I2IIV0_9GAMM
LinkDB: A0A1I2IIV0_9GAMM
Original site: A0A1I2IIV0_9GAMM 
ID   A0A1I2IIV0_9GAMM        Unreviewed;       310 AA.
AC   A0A1I2IIV0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
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=SAMN02799615_03507 {ECO:0000313|EMBL:SFF42269.1};
OS   Dyella marensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Dyella.
OX   NCBI_TaxID=500610 {ECO:0000313|EMBL:SFF42269.1, ECO:0000313|Proteomes:UP000199477};
RN   [1] {ECO:0000313|EMBL:SFF42269.1, ECO:0000313|Proteomes:UP000199477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UNC178MFTsu3.1 {ECO:0000313|EMBL:SFF42269.1,
RC   ECO:0000313|Proteomes:UP000199477};
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   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004948}.
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family.
CC       {ECO:0000256|ARBA:ARBA00005582}.
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DR   EMBL; FONH01000017; SFF42269.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2IIV0; -.
DR   STRING; 500610.SAMN02799615_03507; -.
DR   Proteomes; UP000199477; 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   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd03425; MutT_pyrophosphohydrolase; 1.
DR   CDD; cd00564; TMP_TenI; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
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   InterPro; IPR036206; ThiamineP_synth_sf.
DR   InterPro; IPR022998; ThiamineP_synth_TenI.
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   Pfam; PF02581; TMP-TENI; 1.
DR   PRINTS; PR00502; NUDIXFAMILY.
DR   SUPFAM; SSF55811; Nudix; 1.
DR   SUPFAM; SSF51391; Thiamin phosphate synthase; 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};
KW   Mutator protein {ECO:0000256|ARBA:ARBA00022457};
KW   Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977}.
FT   DOMAIN          1..122
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS51462"
SQ   SEQUENCE   310 AA;  32738 MW;  56F9176A654AFB13 CRC64;
     MAGVLVDPAG RVLLAQRPAG KHLAGTWEFP GGKLEPGETA EAGLARELLE ELGIAIGPAE
     PLTRVPWAYG EKRLLLDAWL LRQWEREPLP LEHEALQWAD PQAVDLAQLA PADRAILQAL
     RLPPHYPITP ADLPPEAFDA CAGMLRDALA RGERLLQLRL PLWPHARLRE LAAALLPEAS
     SRGAQLLLNG DVEGARALGP GIGVQLKASQ LDAWTARPLP WNQPVGASCH DAGELARALG
     AGADFATLSP VAVTATHPDI AAMGWPAFAA LAEAAALPVY ALGGMSAADM ERARAAGGQG
     VAGIRGFWNR
//
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