ID   MUTT_PROVU              Reviewed;         112 AA.
AC   P32090;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=8-oxo-dGTP diphosphatase;
DE            Short=8-oxo-dGTPase;
DE            EC=3.6.1.55 {ECO:0000250|UniProtKB:P08337};
DE   AltName: Full=7,8-dihydro-8-oxoguanine-triphosphatase;
DE   AltName: Full=Mutator protein MutT;
DE   AltName: Full=dGTP pyrophosphohydrolase;
GN   Name=mutT;
OS   Proteus vulgaris.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=585;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8244038; DOI=10.1016/0378-1119(93)90180-b;
RA   Kamath A.V., Yanofsky C.;
RT   "Sequence and characterization of mutT from Proteus vulgaris.";
RL   Gene 134:99-102(1993).
CC   -!- FUNCTION: Specifically hydrolyzes both 8-oxo-deoxyguanosine
CC       triphosphate (8-oxo-dGTP) and 8-oxo-guanosine triphosphate (8-oxo-GTP)
CC       to the related monophosphates, thereby cleaning up the nucleotide pools
CC       and preventing misincorporation of 8-oxoGua into DNA and RNA. It
CC       prevents replicational errors by removing an oxidatively damaged form
CC       of guanine (8-oxo-dGTP) from DNA and the nucleotide pool. 8-oxo-dGTP
CC       can be inserted opposite dA and dC residues of template DNA with almost
CC       equal efficiency thus leading to A.T to G.C transversions.
CC       {ECO:0000250|UniProtKB:P08337}.
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:0000250|UniProtKB:P08337};
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:0000250|UniProtKB:P08337};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P08337};
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR   EMBL; L07579; AAA16277.1; -; Unassigned_DNA.
DR   PIR; JT0675; JT0675.
DR   AlphaFoldDB; P32090; -.
DR   SMR; P32090; -.
DR   GO; GO:0035539; F:8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity; IEA:UniProtKB-EC.
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   InterPro; IPR003561; Mutator_MutT.
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   Pfam; PF00293; NUDIX; 1.
DR   PRINTS; PR01401; MUTATORMUTT.
DR   PRINTS; PR00502; NUDIXFAMILY.
DR   SUPFAM; SSF55811; SSF55811; 1.
DR   TIGRFAMs; TIGR00586; mutt; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA repair; DNA replication; Hydrolase; Magnesium;
KW   Metal-binding; Mutator protein.
FT   CHAIN           1..112
FT                   /note="8-oxo-dGTP diphosphatase"
FT                   /id="PRO_0000056947"
FT   DOMAIN          6..112
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   MOTIF           41..62
FT                   /note="Nudix box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   BINDING         40
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P08337"
FT   BINDING         60
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P08337"
SQ   SEQUENCE   112 AA;  12774 MW;  2C66F00CC378A146 CRC64;
     MMDKKKLHIA AGVICDKHNN VFIAQRPLKS HMGGFWEFPG GKLEDNETPE QALLRELQEE
     IGIDVTQCTL LDTVAHDFPD RHITLSFFLV TEWKNELTEK KGSCRVGHLL CL