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ITPA_BOVIN
ID   ITPA_BOVIN              Reviewed;         208 AA.
AC   Q2KIC5;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 101.
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 {ECO:0000255|HAMAP-Rule:MF_03148};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) 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; BC112688; AAI12689.1; -; mRNA.
DR   RefSeq; NP_001069750.1; NM_001076282.2.
DR   AlphaFoldDB; Q2KIC5; -.
DR   SMR; Q2KIC5; -.
DR   STRING; 9913.ENSBTAP00000018301; -.
DR   PaxDb; Q2KIC5; -.
DR   PRIDE; Q2KIC5; -.
DR   Ensembl; ENSBTAT00000018301; ENSBTAP00000018301; ENSBTAG00000013776.
DR   GeneID; 613653; -.
DR   KEGG; bta:613653; -.
DR   CTD; 3704; -.
DR   VEuPathDB; HostDB:ENSBTAG00000013776; -.
DR   VGNC; VGNC:30342; ITPA.
DR   eggNOG; KOG3222; Eukaryota.
DR   GeneTree; ENSGT00390000015399; -.
DR   HOGENOM; CLU_082080_1_1_1; -.
DR   InParanoid; Q2KIC5; -.
DR   OrthoDB; 1298391at2759; -.
DR   TreeFam; TF105614; -.
DR   Proteomes; UP000009136; Chromosome 13.
DR   Bgee; ENSBTAG00000013776; Expressed in anterior segment of eyeball and 104 other tissues.
DR   ExpressionAtlas; Q2KIC5; baseline and differential.
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   Acetylation; Cytoplasm; Hydrolase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide metabolism; Nucleotide-binding; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03148"
FT   CHAIN           2..208
FT                   /note="Inosine triphosphate pyrophosphatase"
FT                   /id="PRO_0000306869"
FT   BINDING         14..19
FT                   /ligand="ITP"
FT                   /ligand_id="ChEBI:CHEBI:61402"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03148"
FT   BINDING         44
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03148"
FT   BINDING         56
FT                   /ligand="ITP"
FT                   /ligand_id="ChEBI:CHEBI:61402"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03148"
FT   BINDING         72..73
FT                   /ligand="ITP"
FT                   /ligand_id="ChEBI:CHEBI:61402"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03148"
FT   BINDING         89
FT                   /ligand="ITP"
FT                   /ligand_id="ChEBI:CHEBI:61402"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03148"
FT   BINDING         149..152
FT                   /ligand="ITP"
FT                   /ligand_id="ChEBI:CHEBI:61402"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03148"
FT   BINDING         172
FT                   /ligand="ITP"
FT                   /ligand_id="ChEBI:CHEBI:61402"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03148"
FT   BINDING         177..178
FT                   /ligand="ITP"
FT                   /ligand_id="ChEBI:CHEBI:61402"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03148"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BY32, ECO:0000255|HAMAP-
FT                   Rule:MF_03148"
SQ   SEQUENCE   208 AA;  23061 MW;  F49F922F60A8822B CRC64;
     MAASLAGKKI VFVTGNAKKL EEVIQILGDK FPCTLVAQKI DLPEYQGEPD EISIRKCQEA
     ARQVQGPVLV EDTCLCFNAL GGLPGPYIKW FLEKLKPEGL HQLLEGFQDK SAYALCTFAF
     STGDPNEPVR LFRGRTMGRI VVPRGCRDFG WDPCFQPDGY EQTYAEMPKA EKNTISHRFR
     ALLALQEYFS SLTPGVGDDH PSWGSGEG
 
 
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