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Database: UniProt
Entry: E6W0W2_DESIS
LinkDB: E6W0W2_DESIS
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ID   E6W0W2_DESIS            Unreviewed;       197 AA.
AC   E6W0W2;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   RecName: Full=dITP/XTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405};
DE            EC=3.6.1.66 {ECO:0000256|HAMAP-Rule:MF_01405};
DE   AltName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405};
DE   AltName: Full=Non-standard purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405};
DE   AltName: Full=Nucleoside-triphosphate diphosphatase {ECO:0000256|HAMAP-Rule:MF_01405};
DE   AltName: Full=Nucleoside-triphosphate pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405};
DE            Short=NTPase {ECO:0000256|HAMAP-Rule:MF_01405};
GN   OrderedLocusNames=Selin_0546 {ECO:0000313|EMBL:ADU65294.1};
OS   Desulfurispirillum indicum (strain ATCC BAA-1389 / DSM 22839 / S5).
OC   Bacteria; Chrysiogenota; Chrysiogenetes; Chrysiogenales; Chrysiogenaceae;
OC   Desulfurispirillum.
OX   NCBI_TaxID=653733 {ECO:0000313|EMBL:ADU65294.1, ECO:0000313|Proteomes:UP000002572};
RN   [1] {ECO:0000313|EMBL:ADU65294.1, ECO:0000313|Proteomes:UP000002572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1389 / DSM 22839 / S5
RC   {ECO:0000313|Proteomes:UP000002572};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Chertkov O., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Mikhailova N., Haggblom M., Rauschenbach I.,
RA   Bini E., Woyke T.;
RT   "Complete sequence of Desulfurispirillum indicum S5.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01405};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01405};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01405};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01405}.
CC   -!- SIMILARITY: Belongs to the HAM1 NTPase family.
CC       {ECO:0000256|ARBA:ARBA00008023, ECO:0000256|HAMAP-Rule:MF_01405,
CC       ECO:0000256|RuleBase:RU003781}.
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DR   EMBL; CP002432; ADU65294.1; -; Genomic_DNA.
DR   RefSeq; WP_013505182.1; NC_014836.1.
DR   AlphaFoldDB; E6W0W2; -.
DR   STRING; 653733.Selin_0546; -.
DR   KEGG; din:Selin_0546; -.
DR   eggNOG; COG0127; Bacteria.
DR   HOGENOM; CLU_082080_0_3_0; -.
DR   InParanoid; E6W0W2; -.
DR   OMA; YDPIFQP; -.
DR   OrthoDB; 9807456at2; -.
DR   Proteomes; UP000002572; Chromosome.
DR   GO; GO:0035870; F:dITP diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0036220; F:ITP diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:InterPro.
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; IPR029001; ITPase-like_fam.
DR   InterPro; IPR002637; RdgB/HAM1.
DR   NCBIfam; TIGR00042; RdgB/HAM1 family non-canonical purine NTP pyrophosphatase; 1.
DR   PANTHER; PTHR11067:SF9; INOSINE TRIPHOSPHATE PYROPHOSPHATASE; 1.
DR   PANTHER; PTHR11067; INOSINE TRIPHOSPHATE PYROPHOSPHATASE/HAM1 PROTEIN; 1.
DR   Pfam; PF01725; Ham1p_like; 1.
DR   SUPFAM; SSF52972; ITPase-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01405};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01405};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01405}; Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_01405};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01405}; Reference proteome {ECO:0000313|Proteomes:UP000002572}.
FT   ACT_SITE        70
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT   BINDING         7..12
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT   BINDING         41
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT   BINDING         70
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT   BINDING         71
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT   BINDING         150..153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT   BINDING         173
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT   BINDING         178..179
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
SQ   SEQUENCE   197 AA;  21758 MW;  9ED40EBA779C6724 CRC64;
     MKIILASKNR KKLIELREIL RDIGVEVYSP EELEINIPDV EEDGSTFVEN ALKKARSAHL
     YSGLPAIADD SGICVDALGG APGVYSARYA GDHCDDDDNN RKLLDALSEV EDRRGRFACA
     IAYVDDQQSH TVEGFCEGVV LRAPRGEGGF GYDPLFQPTG FEESFGSLPK EVKNRISHRY
     KAIVALKQFL QTVQQPV
//
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