ID A0A1G8KJY9_9PSED Unreviewed; 316 AA.
AC A0A1G8KJY9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=SAMN05216272_10988 {ECO:0000313|EMBL:SDI43757.1};
OS Pseudomonas panipatensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=428992 {ECO:0000313|EMBL:SDI43757.1, ECO:0000313|Proteomes:UP000199636};
RN [1] {ECO:0000313|EMBL:SDI43757.1, ECO:0000313|Proteomes:UP000199636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCM 7469 {ECO:0000313|EMBL:SDI43757.1,
RC ECO:0000313|Proteomes:UP000199636};
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 -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004948}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family.
CC {ECO:0000256|ARBA:ARBA00005582}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FNDS01000009; SDI43757.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8KJY9; -.
DR STRING; 428992.SAMN05216272_10988; -.
DR OrthoDB; 9810648at2; -.
DR Proteomes; UP000199636; 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 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; 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 InterPro; IPR036206; ThiamineP_synth_sf.
DR InterPro; IPR022998; ThiamineP_synth_TenI.
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 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, ECO:0000256|PIRSR:PIRSR603561-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR603561-2};
KW Mutator protein {ECO:0000256|ARBA:ARBA00022457};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977}.
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 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 316 AA; 34062 MW; 8CDD2C2A726B69DA CRC64;
MKRVHVAAAV IRGADGRVLI ARRPDDKHQG GLWEFPGGKV EEGEPVQVAL ARELEEELGI
RVERARPLIR VAHDYPDKQV LLDVWEVSAF SGEPHGAEGQ PLAWVAPRDL PDYEFPAANA
PIVHAARLPE RYLITPEGLE PQALLQGIRA AVGAGIRMIQ LRAPNMFSPE YRDMAVDAVG
LCAGKAQLML KGPLEWLGDF PSAGWHLTAA QLRKYAANGR PFPSERLLAA SCHSAEELAL
ASAMGVDFVT LSPVLPTESH PGEAALGWAA AEQMIAAFNQ PVFLLGGLGP QDVERAWQIG
AQGVAGIRAF WPALEG
//
