MUTX_STRMU
ID MUTX_STRMU Reviewed; 159 AA.
AC P95781;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=8-oxo-dGTP diphosphatase;
DE Short=8-oxo-dGTPase;
DE EC=3.6.1.55;
DE AltName: Full=7,8-dihydro-8-oxoguanine-triphosphatase;
DE AltName: Full=Mutator protein MutT;
DE AltName: Full=dGTP pyrophosphohydrolase;
GN Name=mutX; OrderedLocusNames=SMU_1455;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=XC;
RA Tsukioka Y., Yamashita Y., Nakano Y., Oho T., Koga T.;
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
CC -!- FUNCTION: Involved in the DNA repair system to avoid A.T to G.C
CC transversions. Degrades 8-oxo-dGTP to the monophosphate, but is also
CC active on all of the nucleoside triphosphates (By similarity).
CC {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR EMBL; D78182; BAA11250.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN59114.1; -; Genomic_DNA.
DR RefSeq; NP_721808.1; NC_004350.2.
DR RefSeq; WP_002263089.1; NC_004350.2.
DR AlphaFoldDB; P95781; -.
DR SMR; P95781; -.
DR STRING; 210007.SMU_1455; -.
DR EnsemblBacteria; AAN59114; AAN59114; SMU_1455.
DR KEGG; smu:SMU_1455; -.
DR PATRIC; fig|210007.7.peg.1294; -.
DR eggNOG; COG1051; Bacteria.
DR HOGENOM; CLU_037162_11_2_9; -.
DR OMA; FRADSYN; -.
DR PhylomeDB; P95781; -.
DR Proteomes; UP000002512; Chromosome.
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; IPR003562; Mutator_MutX_prot.
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; PR01402; MUTATORMUTX.
DR SUPFAM; SSF55811; SSF55811; 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..159
FT /note="8-oxo-dGTP diphosphatase"
FT /id="PRO_0000056950"
FT DOMAIN 1..133
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 38..59
FT /note="Nudix box"
FT BINDING 38
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CONFLICT 2
FT /note="T -> I (in Ref. 1; BAA11250)"
FT /evidence="ECO:0000305"
FT CONFLICT 14
FT /note="C -> R (in Ref. 1; BAA11250)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="D -> E (in Ref. 1; BAA11250)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 159 AA; 18850 MW; 3A51D946F95262A0 CRC64;
MTKLATICYI DNGCELLLMH RNKKPNDVHE GKWISVGGKL EKGESPDECA RREIFEETHL
IVKQMDFKGI ITFPDFTPGH DWYTYVFKVR DFEGRLISDK DSREGTLEWV PYNQVLTKPT
WEGDYEIFKW ILDDAPFFSA KFVYQEQKLV DKHVIFYEK
