ID MUTX_STRR6 Reviewed; 154 AA.
AC P59659;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-APR-2003, sequence version 1.
DT 27-MAR-2024, entry version 107.
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=spr1054;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE007317; AAK99858.1; -; Genomic_DNA.
DR RefSeq; NP_358648.1; NC_003098.1.
DR RefSeq; WP_001135782.1; NC_003098.1.
DR AlphaFoldDB; P59659; -.
DR SMR; P59659; -.
DR STRING; 171101.spr1054; -.
DR KEGG; spr:spr1054; -.
DR PATRIC; fig|171101.6.peg.1146; -.
DR eggNOG; COG1051; Bacteria.
DR HOGENOM; CLU_037162_11_2_9; -.
DR Proteomes; UP000000586; 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 CDD; cd03427; MTH1; 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR InterPro; IPR003562; Mutator_MutX_prot.
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 PANTHER; PTHR43758; 7,8-DIHYDRO-8-OXOGUANINE TRIPHOSPHATASE; 1.
DR PANTHER; PTHR43758:SF2; OXIDIZED PURINE NUCLEOSIDE TRIPHOSPHATE HYDROLASE; 1.
DR Pfam; PF00293; NUDIX; 1.
DR PRINTS; PR01402; MUTATORMUTX.
DR PRINTS; PR00502; NUDIXFAMILY.
DR SUPFAM; SSF55811; Nudix; 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..154
FT /note="8-oxo-dGTP diphosphatase"
FT /id="PRO_0000056949"
FT DOMAIN 1..129
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"
SQ SEQUENCE 154 AA; 17870 MW; E177A4B68FE00336 CRC64;
MPQLATICYI DNGKELLMLH RNKKPNDVHE GKWIGVGGKL ERGETPQECA VREILEETGL
KAKPVLKGVI TFPEFTPDLD WYTYVFKVTE FEGDLIDCNE GMLEWVPYDE VLSKPTWEGD
HTFVEWLLED KPFFSAKFVY DGDKLLDTQV DFYE
//
