ID   MUTT_BUCAP              Reviewed;         130 AA.
AC   Q8K9U2;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 103.
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; OrderedLocusNames=BUsg_196;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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; AE013218; AAM67760.1; -; Genomic_DNA.
DR   RefSeq; WP_011053727.1; NC_004061.1.
DR   AlphaFoldDB; Q8K9U2; -.
DR   SMR; Q8K9U2; -.
DR   STRING; 198804.BUsg_196; -.
DR   EnsemblBacteria; AAM67760; AAM67760; BUsg_196.
DR   KEGG; bas:BUsg_196; -.
DR   eggNOG; COG0494; Bacteria.
DR   HOGENOM; CLU_037162_19_2_6; -.
DR   OMA; KLEYQFP; -.
DR   OrthoDB; 1538300at2; -.
DR   Proteomes; UP000000416; Chromosome.
DR   GO; GO:0035539; F:8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity; IEA:UniProtKB-EC.
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; IPR020476; Nudix_hydrolase.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   Pfam; PF00293; NUDIX; 1.
DR   PRINTS; PR00502; NUDIXFAMILY.
DR   SUPFAM; SSF55811; SSF55811; 1.
DR   PROSITE; PS51462; NUDIX; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA repair; DNA replication; Hydrolase; Magnesium;
KW   Metal-binding; Mutator protein.
FT   CHAIN           1..130
FT                   /note="8-oxo-dGTP diphosphatase"
FT                   /id="PRO_0000056945"
FT   DOMAIN          1..128
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   MOTIF           37..58
FT                   /note="Nudix box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   BINDING         36
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P08337"
FT   BINDING         56
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P08337"
SQ   SEQUENCE   130 AA;  16090 MW;  FB8A3C8FCB9A042F CRC64;
     MKYTNIVIGI IIKKNKIYIT KARKKKYVLD LWEFPGGKVK ENENLTYSLK RELSEEVGLK
     ILRFRFFRCI KYFYKKIKLY FFLITRWKGR IYSKEGYLYK WIFLDDLKYF NFPSPNSHII
     HDLQKMIFFK