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Database: UniProt
Entry: A0A071M1J8_9ENTR
LinkDB: A0A071M1J8_9ENTR
Original site: A0A071M1J8_9ENTR 
ID   A0A071M1J8_9ENTR        Unreviewed;       197 AA.
AC   A0A071M1J8;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 40.
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=DT73_01500 {ECO:0000313|EMBL:KEA54577.1};
OS   Mangrovibacter sp. MFB070.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Mangrovibacter.
OX   NCBI_TaxID=1224318 {ECO:0000313|EMBL:KEA54577.1, ECO:0000313|Proteomes:UP000027726};
RN   [1] {ECO:0000313|EMBL:KEA54577.1, ECO:0000313|Proteomes:UP000027726}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MFB070 {ECO:0000313|EMBL:KEA54577.1,
RC   ECO:0000313|Proteomes:UP000027726};
RA   Joseph T.C., Varghese A.M., Baby A., Reghunathan D., V M., Lalitha K.V.;
RT   "Draft Genome Sequence of Mangrovibacter spp. MFB070 a Nitrogen-fixing
RT   Bacterium Isolated from an Aquaculture Farm.";
RL   Submitted (APR-2014) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KEA54577.1}.
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DR   EMBL; JJMI01000002; KEA54577.1; -; Genomic_DNA.
DR   RefSeq; WP_036102870.1; NZ_JJMI01000002.1.
DR   AlphaFoldDB; A0A071M1J8; -.
DR   eggNOG; COG0127; Bacteria.
DR   Proteomes; UP000027726; Unassembled WGS sequence.
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};
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:UP000027726}.
FT   ACT_SITE        69
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT   BINDING         8..13
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT   BINDING         40
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT   BINDING         69
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT   BINDING         70
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   197 AA;  21057 MW;  0A48EBDCE7FBCC08 CRC64;
     MQKVVLATGN AGKVRELADL LENFGLDIVA QTELGVDSAE ETGGTFIENA ILKARHAARI
     TGLPAIADDS GLAVDALGGA PGIYSARYAG EEATDQQNLE KLLHTMDSVP DNLRKARFHC
     VLVYMRHADD PTPLVCHGSW EGEITRVPAG QGGFGYDPIF YVASEGKTAA ELTKEEKRAI
     SHRGQALALL LEAMRNG
//
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