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IXTPA_STRP6
ID   IXTPA_STRP6             Reviewed;         328 AA.
AC   Q5XDP8;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 2.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=dITP/XTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01405};
DE            EC=3.6.1.66 {ECO:0000255|HAMAP-Rule:MF_01405};
DE   AltName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01405};
DE   AltName: Full=Non-standard purine NTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01405};
DE   AltName: Full=Nucleoside-triphosphate diphosphatase {ECO:0000255|HAMAP-Rule:MF_01405};
DE   AltName: Full=Nucleoside-triphosphate pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01405};
DE            Short=NTPase {ECO:0000255|HAMAP-Rule:MF_01405};
GN   OrderedLocusNames=M6_Spy0330;
OS   Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=286636;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-946 / MGAS10394;
RX   PubMed=15272401; DOI=10.1086/422697;
RA   Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA   Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT   "Progress toward characterization of the group A Streptococcus metagenome:
RT   complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL   J. Infect. Dis. 190:727-738(2004).
CC   -!- FUNCTION: Pyrophosphatase that catalyzes the hydrolysis of nucleoside
CC       triphosphates to their monophosphate derivatives, with a high
CC       preference for the non-canonical purine nucleotides XTP (xanthosine
CC       triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to
CC       function as a house-cleaning enzyme that removes non-canonical purine
CC       nucleotides from the nucleotide pool, thus preventing their
CC       incorporation into DNA/RNA and avoiding chromosomal lesions.
CC       {ECO:0000255|HAMAP-Rule:MF_01405}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + XTP = diphosphate + H(+) + XMP; Xref=Rhea:RHEA:28610,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57464, ChEBI:CHEBI:61314; EC=3.6.1.66;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01405};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dITP + H2O = dIMP + diphosphate + H(+); Xref=Rhea:RHEA:28342,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:61194, ChEBI:CHEBI:61382; EC=3.6.1.66;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01405};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + ITP = diphosphate + H(+) + IMP; Xref=Rhea:RHEA:29399,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58053, ChEBI:CHEBI:61402; EC=3.6.1.66;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01405};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01405};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01405};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01405}.
CC   -!- SIMILARITY: Belongs to the HAM1 NTPase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01405, ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAT86465.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000003; AAT86465.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011184197.1; NC_006086.1.
DR   AlphaFoldDB; Q5XDP8; -.
DR   SMR; Q5XDP8; -.
DR   EnsemblBacteria; AAT86465; AAT86465; M6_Spy0330.
DR   KEGG; spa:M6_Spy0330; -.
DR   HOGENOM; CLU_863088_0_0_9; -.
DR   Proteomes; UP000001167; Chromosome.
DR   GO; GO:0035870; F:dITP diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0036220; F:ITP diphosphatase activity; IEA:RHEA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0036222; F:XTP diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009146; P:purine nucleoside triphosphate catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00515; HAM1; 1.
DR   Gene3D; 3.90.950.10; -; 1.
DR   HAMAP; MF_01405; Non_canon_purine_NTPase; 1.
DR   InterPro; IPR020922; dITP/XTP_pyrophosphatase.
DR   InterPro; IPR002637; Ham1p-like.
DR   InterPro; IPR029001; ITPase-like_fam.
DR   PANTHER; PTHR11067; PTHR11067; 1.
DR   Pfam; PF01725; Ham1p_like; 1.
DR   SUPFAM; SSF52972; SSF52972; 1.
DR   TIGRFAMs; TIGR00042; TIGR00042; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW   Nucleotide-binding.
FT   CHAIN           1..328
FT                   /note="dITP/XTP pyrophosphatase"
FT                   /id="PRO_0000178244"
FT   REGION          1..129
FT                   /note="Unknown"
FT   REGION          130..324
FT                   /note="NTP pyrophosphatase"
FT   ACT_SITE        196
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01405"
FT   BINDING         134..139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01405"
FT   BINDING         196
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01405"
FT   BINDING         197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01405"
FT   BINDING         280..283
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01405"
FT   BINDING         303
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01405"
FT   BINDING         308..309
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01405"
SQ   SEQUENCE   328 AA;  36445 MW;  8C05ED79DA7662B8 CRC64;
     MSEKIYEYKD ENNWFIGKMT GHNLISGWGV KHRTIKKIDD LLDGIAATLD WENPKGYDVS
     VVRYQSPLSL ITFIIDMINQ ETQREIKVIP HAGTILLMEN AKLLAVYLPE GGVSTATFFA
     TSEQGFGDTI LIATRNEGKT KEFRNLFGQL GYRVENLNDY PELPEVAETG TTFEENARLK
     AETISHLTGK MVLADDSGLK VDALGDLPGV WSARFSGPDA TDAKNNAKLL HELAMVFDQK
     KRSAQFHTTL VVAAPNKDSL VVEAEWPGYI ATQPKGENGF GYDPVFIVGE TGRHAAELEA
     DQKNQLSHRG QAVRKLMEVF PAWQAKQS
 
 
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