ITPA_XENLA
ID ITPA_XENLA Reviewed; 195 AA.
AC Q2NLA8;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Inosine triphosphate pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_03148};
DE Short=ITPase {ECO:0000255|HAMAP-Rule:MF_03148};
DE Short=Inosine triphosphatase {ECO:0000255|HAMAP-Rule:MF_03148};
DE EC=3.6.1.9 {ECO:0000255|HAMAP-Rule:MF_03148};
DE AltName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_03148};
DE AltName: Full=Non-standard purine NTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_03148};
DE AltName: Full=Nucleoside-triphosphate diphosphatase {ECO:0000255|HAMAP-Rule:MF_03148};
DE AltName: Full=Nucleoside-triphosphate pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_03148};
DE Short=NTPase {ECO:0000255|HAMAP-Rule:MF_03148};
GN Name=itpa;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Pyrophosphatase that hydrolyzes the non-canonical purine
CC nucleotides inosine triphosphate (ITP), deoxyinosine triphosphate
CC (dITP) as well as 2'-deoxy-N-6-hydroxylaminopurine triphosphate
CC (dHAPTP) and xanthosine 5'-triphosphate (XTP) to their respective
CC monophosphate derivatives. The enzyme does not distinguish between the
CC deoxy- and ribose forms. Probably excludes non-canonical purines from
CC RNA and DNA precursor pools, thus preventing their incorporation into
CC RNA and DNA and avoiding chromosomal lesions. {ECO:0000255|HAMAP-
CC Rule:MF_03148}.
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:0000255|HAMAP-Rule:MF_03148};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23997;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03148};
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:0000255|HAMAP-Rule:MF_03148};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44645;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03148};
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:0000255|HAMAP-Rule:MF_03148};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29400;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03148};
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:0000255|HAMAP-Rule:MF_03148};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28343;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03148};
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:0000255|HAMAP-Rule:MF_03148};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28611;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03148};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03148};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03148};
CC Note=Binds 1 divalent metal cation per subunit; can use either Mg(2+)
CC or Mn(2+). {ECO:0000255|HAMAP-Rule:MF_03148};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03148}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03148}.
CC -!- SIMILARITY: Belongs to the HAM1 NTPase family. {ECO:0000255|HAMAP-
CC Rule:MF_03148}.
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DR EMBL; BC110771; AAI10772.1; -; mRNA.
DR RefSeq; NP_001089939.1; NM_001096470.1.
DR AlphaFoldDB; Q2NLA8; -.
DR SMR; Q2NLA8; -.
DR DNASU; 735008; -.
DR GeneID; 735008; -.
DR KEGG; xla:735008; -.
DR CTD; 735008; -.
DR Xenbase; XB-GENE-1001458; itpa.S.
DR OMA; DCFADDT; -.
DR OrthoDB; 1298391at2759; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 735008; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; 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:0009204; P:deoxyribonucleoside triphosphate catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00515; HAM1; 1.
DR Gene3D; 3.90.950.10; -; 1.
DR HAMAP; MF_03148; HAM1_NTPase; 1.
DR InterPro; IPR002637; Ham1p-like.
DR InterPro; IPR027502; ITPase.
DR InterPro; IPR029001; ITPase-like_fam.
DR PANTHER; PTHR11067; PTHR11067; 1.
DR Pfam; PF01725; Ham1p_like; 1.
DR SUPFAM; SSF52972; SSF52972; 1.
DR TIGRFAMs; TIGR00042; TIGR00042; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Nucleotide metabolism; Nucleotide-binding; Reference proteome.
FT CHAIN 1..195
FT /note="Inosine triphosphate pyrophosphatase"
FT /id="PRO_0000413104"
FT BINDING 13..18
FT /ligand="ITP"
FT /ligand_id="ChEBI:CHEBI:61402"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03148"
FT BINDING 43
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03148"
FT BINDING 55
FT /ligand="ITP"
FT /ligand_id="ChEBI:CHEBI:61402"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03148"
FT BINDING 71..72
FT /ligand="ITP"
FT /ligand_id="ChEBI:CHEBI:61402"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03148"
FT BINDING 88
FT /ligand="ITP"
FT /ligand_id="ChEBI:CHEBI:61402"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03148"
FT BINDING 148..151
FT /ligand="ITP"
FT /ligand_id="ChEBI:CHEBI:61402"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03148"
FT BINDING 171
FT /ligand="ITP"
FT /ligand_id="ChEBI:CHEBI:61402"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03148"
FT BINDING 176..177
FT /ligand="ITP"
FT /ligand_id="ChEBI:CHEBI:61402"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03148"
SQ SEQUENCE 195 AA; 21803 MW; FC89988B6DF36838 CRC64;
MAAAAGRSIV FVTGNAKKLE EVVQILGDKF PCKLVAKKID LPEYQGEPDE ISIQKCREAA
KQIQGPVIVE DTCLCFNALG GLPGPYIKWF LEKIKPEGLH RMLEGFEDKS AIALCTFAYC
NGNPDDTVLL FRGKTLGQIV LPRGPRDFGW DPCFQPDGFQ QTYAELPKEV KNTISHRYRA
LKEMSDYFIQ NGTKV
