ITPA_ENCIT
ID ITPA_ENCIT Reviewed; 194 AA.
AC E0S6S0;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Inosine triphosphate pyrophosphatase;
DE Short=ITPase;
DE Short=Inosine triphosphatase;
DE EC=3.6.1.9 {ECO:0000250|UniProtKB:Q9BY32};
DE AltName: Full=Non-canonical purine NTP pyrophosphatase;
DE AltName: Full=Non-standard purine NTP pyrophosphatase;
DE AltName: Full=Nucleoside-triphosphate diphosphatase;
DE AltName: Full=Nucleoside-triphosphate pyrophosphatase;
DE Short=NTPase;
GN ORFNames=Eint_041160;
OS Encephalitozoon intestinalis (strain ATCC 50506) (Microsporidian parasite)
OS (Septata intestinalis).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=876142;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50506;
RX PubMed=20865802; DOI=10.1038/ncomms1082;
RA Corradi N., Pombert J.-F., Farinelli L., Didier E.S., Keeling P.J.;
RT "The complete sequence of the smallest known nuclear genome from the
RT microsporidian Encephalitozoon intestinalis.";
RL Nat. Commun. 1:77-77(2010).
CC -!- FUNCTION: Pyrophosphatase that hydrolyzes non-canonical purine
CC nucleotides such as inosine triphosphate (ITP), deoxyinosine
CC triphosphate (dITP) or xanthosine 5'-triphosphate (XTP) to their
CC respective monophosphate derivatives. The enzyme does not distinguish
CC between the deoxy- and ribose forms. Probably excludes non-canonical
CC purines from RNA and DNA precursor pools, thus preventing their
CC incorporation into RNA and DNA and avoiding chromosomal lesions.
CC {ECO:0000250|UniProtKB:Q9BY32}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC phosphate + diphosphate + H(+); Xref=Rhea:RHEA:23996,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.9;
CC Evidence={ECO:0000250|UniProtKB:Q9BY32};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23997;
CC Evidence={ECO:0000250|UniProtKB:Q9BY32};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'-
CC deoxyribonucleoside 5'-phosphate + diphosphate + H(+);
CC Xref=Rhea:RHEA:44644, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:65317; EC=3.6.1.9;
CC Evidence={ECO:0000250|UniProtKB:Q9BY32};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44645;
CC Evidence={ECO:0000250|UniProtKB:Q9BY32};
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=3.6.1.9;
CC Evidence={ECO:0000250|UniProtKB:Q9BY32};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29400;
CC Evidence={ECO:0000250|UniProtKB:Q9BY32};
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=3.6.1.9;
CC Evidence={ECO:0000250|UniProtKB:Q9BY32};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28343;
CC Evidence={ECO:0000250|UniProtKB:Q9BY32};
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=3.6.1.9;
CC Evidence={ECO:0000250|UniProtKB:Q9BY32};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28611;
CC Evidence={ECO:0000250|UniProtKB:Q9BY32};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9BY32};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9BY32};
CC Note=Binds 1 divalent metal cation per subunit; can use either Mg(2+)
CC or Mn(2+). {ECO:0000250|UniProtKB:Q9BY32};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9BY32}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BY32}. Nucleus
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HAM1 NTPase family. {ECO:0000305}.
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DR EMBL; CP001945; ADM11405.1; -; Genomic_DNA.
DR RefSeq; XP_003072765.1; XM_003072719.1.
DR AlphaFoldDB; E0S6S0; -.
DR SMR; E0S6S0; -.
DR EnsemblFungi; ADM11405; ADM11405; Eint_041160.
DR GeneID; 9699006; -.
DR KEGG; ein:Eint_041160; -.
DR VEuPathDB; MicrosporidiaDB:Eint_041160; -.
DR HOGENOM; CLU_082080_1_0_1; -.
DR OrthoDB; 1298391at2759; -.
DR Proteomes; UP000002313; Chromosome IV.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0035870; F:dITP diphosphatase activity; IEA:RHEA.
DR GO; GO:0036218; F:dTTP 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:0035529; F:NADH pyrophosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0036222; F:XTP diphosphatase activity; IEA:RHEA.
DR GO; GO:0009143; P:nucleoside triphosphate catabolic process; IEA:InterPro.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00515; HAM1; 1.
DR Gene3D; 3.90.950.10; -; 1.
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.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Nucleotide metabolism; Nucleotide-binding; Nucleus.
FT CHAIN 1..194
FT /note="Inosine triphosphate pyrophosphatase"
FT /id="PRO_0000413140"
FT BINDING 10..15
FT /ligand="ITP"
FT /ligand_id="ChEBI:CHEBI:61402"
FT /evidence="ECO:0000250|UniProtKB:Q9BY32"
FT BINDING 36
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9BY32"
FT BINDING 48
FT /ligand="ITP"
FT /ligand_id="ChEBI:CHEBI:61402"
FT /evidence="ECO:0000250|UniProtKB:Q9BY32"
FT BINDING 66..67
FT /ligand="ITP"
FT /ligand_id="ChEBI:CHEBI:61402"
FT /evidence="ECO:0000250|UniProtKB:Q9BY32"
FT BINDING 83
FT /ligand="ITP"
FT /ligand_id="ChEBI:CHEBI:61402"
FT /evidence="ECO:0000250|UniProtKB:Q9BY32"
FT BINDING 166
FT /ligand="ITP"
FT /ligand_id="ChEBI:CHEBI:61402"
FT /evidence="ECO:0000250|UniProtKB:Q9BY32"
FT BINDING 171..172
FT /ligand="ITP"
FT /ligand_id="ChEBI:CHEBI:61402"
FT /evidence="ECO:0000250|UniProtKB:Q9BY32"
SQ SEQUENCE 194 AA; 21455 MW; C560A6C44B65EF91 CRC64;
MTTGKIYFAT TNLKKLNEVK EFLKTDIDHM RISMTEIQGP SEKIVEHKLD QAAPFINPKD
AVIVDDTSFS LEALGGFPGV YVKDFLEIGT RKIWEIVEKI GNKSATAVCS LGIAHYENGE
IVKKVFSGKL KGSITEPEKD CKTEFGYIFI PDGFNGVLKN MPTDEKNRIS HRGIASRSLA
AYMASKGIIK THGP
