ID   MUTT_HAEIN              Reviewed;         136 AA.
AC   P44932;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 126.
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=HI_0910;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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; L42023; AAC22567.1; -; Genomic_DNA.
DR   RefSeq; NP_439070.1; NC_000907.1.
DR   RefSeq; WP_010869085.1; NC_000907.1.
DR   AlphaFoldDB; P44932; -.
DR   SMR; P44932; -.
DR   STRING; 71421.HI_0910; -.
DR   EnsemblBacteria; AAC22567; AAC22567; HI_0910.
DR   KEGG; hin:HI_0910; -.
DR   PATRIC; fig|71421.8.peg.951; -.
DR   eggNOG; COG0494; Bacteria.
DR   HOGENOM; CLU_037162_19_2_6; -.
DR   OMA; KLEYQFP; -.
DR   PhylomeDB; P44932; -.
DR   BioCyc; HINF71421:G1GJ1-949-MON; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0035539; F:8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity; IBA:GO_Central.
DR   GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IBA:GO_Central.
DR   GO; GO:0044715; F:8-oxo-dGDP phosphatase activity; IBA:GO_Central.
DR   GO; GO:0044716; F:8-oxo-GDP phosphatase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..136
FT                   /note="8-oxo-dGTP diphosphatase"
FT                   /id="PRO_0000056946"
FT   DOMAIN          4..130
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   MOTIF           40..61
FT                   /note="Nudix box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   BINDING         39
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P08337"
FT   BINDING         59
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P08337"
SQ   SEQUENCE   136 AA;  15648 MW;  67F80E6EAC5D17F4 CRC64;
     MDKKIIQVAA GIIRNEFGQI YLTQRLEGQD FAQSLEFPGG KVDAGETPEQ ALKRELEEEI
     GIVALNAELY ERFQFEYPTK IISFFFYLVN EWIGEPFGRE GQEGFWVEQH ALDAGQFPPA
     NAKLIHRLLN ETHNFI