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Entry: A0A2W7I2M5_9PROT
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ID   A0A2W7I2M5_9PROT        Unreviewed;       323 AA.
AC   A0A2W7I2M5;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
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=C8P66_12263 {ECO:0000313|EMBL:PZW41076.1};
OS   Humitalea rosea.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Humitalea.
OX   NCBI_TaxID=990373 {ECO:0000313|EMBL:PZW41076.1, ECO:0000313|Proteomes:UP000249688};
RN   [1] {ECO:0000313|EMBL:PZW41076.1, ECO:0000313|Proteomes:UP000249688}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24525 {ECO:0000313|EMBL:PZW41076.1,
RC   ECO:0000313|Proteomes:UP000249688};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (JUN-2018) 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}.
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:PZW41076.1}.
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DR   EMBL; QKYU01000022; PZW41076.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2W7I2M5; -.
DR   OrthoDB; 9810648at2; -.
DR   Proteomes; UP000249688; Unassembled WGS sequence.
DR   GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; 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; 3.40.630.30; -; 1.
DR   Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
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; PF13302; Acetyltransf_3; 1.
DR   Pfam; PF14815; NUDIX_4; 1.
DR   PRINTS; PR00502; NUDIXFAMILY.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF55811; Nudix; 1.
DR   PROSITE; PS51186; GNAT; 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   Reference proteome {ECO:0000313|Proteomes:UP000249688}.
FT   DOMAIN          12..178
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
FT   DOMAIN          192..321
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS51462"
FT   BINDING         214
FT                   /ligand="8-oxo-dGTP"
FT                   /ligand_id="ChEBI:CHEBI:77896"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603561-1"
FT   BINDING         225..228
FT                   /ligand="8-oxo-dGTP"
FT                   /ligand_id="ChEBI:CHEBI:77896"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603561-1"
FT   BINDING         228
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603561-2"
FT   BINDING         248
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603561-2"
SQ   SEQUENCE   323 AA;  35088 MW;  62B027AD533495C7 CRC64;
     MPGFAPLVTS RLLLRPLRPE DAPDLHRLVN DWDIAKNLAH VPFPYPRDLA DRWIADTAER
     LAAGRGYSLA IERDGALVGC IGLTMAGEEA ELGYWIGRRY WGQGLAAEAA GRLAAWALAT
     LPLRRIRAEA LVDNARSIAV LRRIGFSEAG EGEAEFASRG GMMPVLRFVA TRESLPALAP
     TPVAPVAEAP GLRILLVAAC ALIDSDGRVL LARRPEGKPL AGLWEFPGGK VAPGETPEDA
     LIRELQEELG IEVASPCLAP FTFASHAYPG FHLLMPLYLC RRWQGKVTGR EGQALAWVRP
     DKLGTYQMPP ADVPLVALLR DFL
//
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