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Database: UniProt
Entry: NTDP_STRMU
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Original site: NTDP_STRMU 
ID   NTDP_STRMU              Reviewed;         177 AA.
AC   Q8DSK1;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   18-JUN-2025, entry version 95.
DE   RecName: Full=Nucleoside triphosphate/diphosphate phosphatase {ECO:0000255|HAMAP-Rule:MF_01568};
DE            EC=3.6.1.15 {ECO:0000255|HAMAP-Rule:MF_01568};
DE            EC=3.6.1.6 {ECO:0000255|HAMAP-Rule:MF_01568};
GN   OrderedLocusNames=SMU_1781;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
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: Has nucleoside phosphatase activity towards nucleoside
CC       triphosphates and nucleoside diphosphates. {ECO:0000255|HAMAP-
CC       Rule:MF_01568}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC         diphosphate + phosphate + H(+); Xref=Rhea:RHEA:23680,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01568};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-diphosphate + H2O = a ribonucleoside 5'-
CC         phosphate + phosphate + H(+); Xref=Rhea:RHEA:36799,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:58043; EC=3.6.1.6;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01568};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01568};
CC   -!- SIMILARITY: Belongs to the Ntdp family. {ECO:0000255|HAMAP-
CC       Rule:MF_01568}.
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DR   EMBL; AE014133; AAN59408.1; -; Genomic_DNA.
DR   RefSeq; NP_722102.1; NC_004350.2.
DR   RefSeq; WP_002263684.1; NC_004350.2.
DR   AlphaFoldDB; Q8DSK1; -.
DR   SMR; Q8DSK1; -.
DR   STRING; 210007.SMU_1781; -.
DR   KEGG; smu:SMU_1781; -.
DR   PATRIC; fig|210007.7.peg.1589; -.
DR   eggNOG; COG3557; Bacteria.
DR   HOGENOM; CLU_109787_1_0_9; -.
DR   OrthoDB; 1645325at2; -.
DR   PhylomeDB; Q8DSK1; -.
DR   Proteomes; UP000002512; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0017110; F:nucleoside diphosphate phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.40.380.10; FomD-like; 1.
DR   HAMAP; MF_01568; Ntdp; 1.
DR   InterPro; IPR007295; DUF402.
DR   InterPro; IPR035930; FomD-like_sf.
DR   InterPro; IPR050212; Ntdp-like.
DR   InterPro; IPR016882; SA1684.
DR   NCBIfam; NF010183; PRK13662.1; 1.
DR   PANTHER; PTHR39159; -; 1.
DR   PANTHER; PTHR39159:SF1; UPF0374 PROTEIN YGAC; 1.
DR   Pfam; PF04167; DUF402; 1.
DR   PIRSF; PIRSF028345; UCP028345; 1.
DR   SUPFAM; SSF159234; FomD-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..177
FT                   /note="Nucleoside triphosphate/diphosphate phosphatase"
FT                   /id="PRO_0000248120"
FT   ACT_SITE        23
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01568"
FT   BINDING         87
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01568"
FT   BINDING         103
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01568"
FT   BINDING         105
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01568"
FT   BINDING         107
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01568"
FT   BINDING         107
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01568"
FT   BINDING         120
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01568"
FT   BINDING         123
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01568"
SQ   SEQUENCE   177 AA;  21005 MW;  8F8D3E04B5EF19FA CRC64;
     MKLPKEGDFI TIQSYKHDGS LHRTWRDTMV LKTTENAVIG VNDHTLVTES DGRRWVTREP
     AIVYFHKKFW FNIIAMIRDN GVSYYCNLAS PYIMDQEALK YIDYDLDVKV FADGEKKLLD
     VDEYELHKQK MGYSSDIDYI LKENVKILVD WINNGKGPFS QSYINIWYKR YLELKNR
//
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