ID   F2K025_MARM1            Unreviewed;       202 AA.
AC   F2K025;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   04-NOV-2026, entry version 69.
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=Marme_4031 {ECO:0000313|EMBL:ADZ93239.1};
OS   Marinomonas mediterranea (strain ATCC 700492 / JCM 21426 / NBRC 103028 /
OS   MMB-1).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Oceanospirillales; Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=717774 {ECO:0000313|EMBL:ADZ93239.1, ECO:0000313|Proteomes:UP000001062};
RN   [1] {ECO:0000313|EMBL:ADZ93239.1, ECO:0000313|Proteomes:UP000001062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1
RC   {ECO:0000313|Proteomes:UP000001062};
RX   PubMed=22675599; DOI=10.4056/sigs.2545743;
RA   Lucas-Elio P., Goodwin L., Woyke T., Pitluck S., Nolan M., Kyrpides N.C.,
RA   Detter J.C., Copeland A., Teshima H., Bruce D., Detter C., Tapia R.,
RA   Han S., Land M.L., Ivanova N., Mikhailova N., Johnston A.W.,
RA   Sanchez-Amat A.;
RT   "Complete genome sequence of the melanogenic marine bacterium Marinomonas
RT   mediterranea type strain (MMB-1(T)).";
RL   Stand. Genomic Sci. 6:63-73(2012).
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=ITP + H2O = IMP + diphosphate + H(+); 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=XTP + H2O = XMP + diphosphate + H(+); 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|ARBA:ARBA00052017, ECO:0000256|HAMAP-
CC         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|ARBA:ARBA00051875, ECO:0000256|HAMAP-
CC         Rule:MF_01405};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01405};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01405};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC       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; CP002583; ADZ93239.1; -; Genomic_DNA.
DR   RefSeq; WP_013663141.1; NC_015276.1.
DR   AlphaFoldDB; F2K025; -.
DR   STRING; 717774.Marme_4031; -.
DR   KEGG; mme:Marme_4031; -.
DR   PATRIC; fig|717774.3.peg.4159; -.
DR   eggNOG; COG0127; Bacteria.
DR   HOGENOM; CLU_082080_0_3_6; -.
DR   OMA; AADPCPI; -.
DR   OrthoDB; 9807456at2; -.
DR   Proteomes; UP000001062; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0035870; F:dITP diphosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0036220; F:ITP diphosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:InterPro.
DR   GO; GO:0036222; F:XTP diphosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009146; P:purine nucleoside triphosphate catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00515; HAM1; 1.
DR   FunFam; 3.90.950.10:FF:000001; dITP/XTP pyrophosphatase; 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};
KW   Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080, ECO:0000256|HAMAP-
KW   Rule:MF_01405};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01405}; Reference proteome {ECO:0000313|Proteomes:UP000001062}.
FT   ACT_SITE        70
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT   BINDING         9..14
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         155..158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT   BINDING         178
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT   BINDING         183..184
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
SQ   SEQUENCE   202 AA;  22022 MW;  23CAF42FD632653D CRC64;
     MNKTIVLASN NSGKIKEFNS LFSQYGIDVK PQGEFNVEEA DETGLSFIEN AILKARNACA
     RTNLPAIADD SGIEVDYLNG APGIYSARFA GEHGDNDANN ALLLEKLDGV PTEQRTARFH
     CVLAYMRHKD DPTPIVVQGS WEGRILESNE GVEGFGYDPI FFVPEQGCSS ASLPKEVKNS
     LSHRAKALKL LMAAFKEKSV LA
//