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Database: UniProt
Entry: H0UIM1_9BACT
LinkDB: H0UIM1_9BACT
Original site: H0UIM1_9BACT 
ID   H0UIM1_9BACT            Unreviewed;       203 AA.
AC   H0UIM1;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 51.
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   ORFNames=JonanDRAFT_1402 {ECO:0000313|EMBL:EHM13766.1};
OS   Jonquetella anthropi DSM 22815.
OC   Bacteria; Synergistota; Synergistia; Synergistales;
OC   Dethiosulfovibrionaceae; Jonquetella.
OX   NCBI_TaxID=885272 {ECO:0000313|EMBL:EHM13766.1, ECO:0000313|Proteomes:UP000003806};
RN   [1] {ECO:0000313|EMBL:EHM13766.1, ECO:0000313|Proteomes:UP000003806}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22815 {ECO:0000313|EMBL:EHM13766.1,
RC   ECO:0000313|Proteomes:UP000003806};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Held B.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The Noncontiguous Finished genome of Jonquetella anthropi DSM 22815.";
RL   Submitted (NOV-2011) 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; CM001376; EHM13766.1; -; Genomic_DNA.
DR   RefSeq; WP_008519459.1; NZ_CM001376.1.
DR   AlphaFoldDB; H0UIM1; -.
DR   STRING; 885272.JonanDRAFT_1402; -.
DR   eggNOG; COG0127; Bacteria.
DR   HOGENOM; CLU_082080_0_2_0; -.
DR   OrthoDB; 9807456at2; -.
DR   Proteomes; UP000003806; 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:UP000003806}.
FT   ACT_SITE        76
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT   BINDING         14..19
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT   BINDING         47
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT   BINDING         76
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT   BINDING         77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT   BINDING         154..157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT   BINDING         177
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT   BINDING         182..183
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
SQ   SEQUENCE   203 AA;  22103 MW;  173FED5A851D729F CRC64;
     MIDVKTLRQL VIATGNRNKF VEFQKLLAPL GITLLMGKDL CPNLEVEETG ETFLENARLK
     AQAWCERTNL PALADDSGIE VAALGGRPGV RSARYAPTDA ECRAKLLGEL AGVADRSARF
     AAALVLCWPD GSEWSTLQYC DGSVTEQELG ERGFGYDSLF LPLGETKTFA QMTMEEKDAV
     SHRGKATRQL FLALGGKCDT IKS
//
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