MUTX_STRPN
ID MUTX_STRPN Reviewed; 154 AA.
AC P41354;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 129.
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=SP_1168;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=R6 / R800;
RX PubMed=8170394; DOI=10.1111/j.1365-2958.1994.tb00312.x;
RA Mejean V., Salles C., Bullions L.C., Bessman M.J., Claverys J.-P.;
RT "Characterization of the mutX gene of Streptococcus pneumoniae as a
RT homologue of Escherichia coli mutT, and tentative definition of a catalytic
RT domain of the dGTP pyrophosphohydrolases.";
RL Mol. Microbiol. 11:323-330(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [3]
RP CHARACTERIZATION.
RX PubMed=8163538; DOI=10.1016/s0021-9258(17)32721-7;
RA Bullions L.C., Mejean V., Claverys J.-P., Bessman M.J.;
RT "Purification of the MutX protein of Streptococcus pneumoniae, a homologue
RT of Escherichia coli MutT. Identification of a novel catalytic domain for
RT nucleoside triphosphate pyrophosphohydrolase activity.";
RL J. Biol. Chem. 269:12339-12344(1994).
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.
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;
CC -!- SUBUNIT: Homotrimer.
CC -!- INTERACTION:
CC P41354; P95830: dnaJ; NbExp=2; IntAct=EBI-2207232, EBI-2207079;
CC P41354; Q97SE5: gatC; NbExp=2; IntAct=EBI-2207232, EBI-2207053;
CC P41354; Q97NV3: groES; NbExp=2; IntAct=EBI-2207232, EBI-2206949;
CC P41354; Q97S73: grpE; NbExp=2; IntAct=EBI-2207232, EBI-2207065;
CC P41354; Q97SR4: uppS; NbExp=2; IntAct=EBI-2207232, EBI-2206983;
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR EMBL; Z21702; CAA79807.1; -; Genomic_DNA.
DR EMBL; AE005672; AAK75277.1; -; Genomic_DNA.
DR PIR; D95135; D95135.
DR PIR; F98003; F98003.
DR PIR; S41532; S41532.
DR RefSeq; WP_001135768.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; P41354; -.
DR SMR; P41354; -.
DR IntAct; P41354; 5.
DR STRING; 170187.SP_1168; -.
DR EnsemblBacteria; AAK75277; AAK75277; SP_1168.
DR GeneID; 61380500; -.
DR KEGG; spn:SP_1168; -.
DR eggNOG; COG1051; Bacteria.
DR OMA; FRADSYN; -.
DR PhylomeDB; P41354; -.
DR BioCyc; SPNE170187:G1FZB-1188-MON; -.
DR Proteomes; UP000000585; 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; 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; PR01402; MUTATORMUTX.
DR PRINTS; PR00502; NUDIXFAMILY.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; DNA replication; Hydrolase; Magnesium;
KW Metal-binding; Mutator protein.
FT CHAIN 1..154
FT /note="8-oxo-dGTP diphosphatase"
FT /id="PRO_0000056948"
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"
FT CONFLICT 51
FT /note="A -> V (in Ref. 1; CAA79807)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="T -> M (in Ref. 1; CAA79807)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 154 AA; 17812 MW; E95F063CB4CC8EE0 CRC64;
MPQLATICYI DNGKELLMLH RNKKPNDVHE GKWIGVGGKL ERGETPQECA AREILEETGL
KAKPVLKGVI TFPEFTPDLD WYTYVFKVTE FEGDLIDCNE GTLEWVPYDE VLSKPTWEGD
HTFVEWLLED KPFFSAKFVY DGDKLLDTQV DFYE
