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Inosine triphosphate pyrophosphatase (ITPase) (Inosine triphosphatase) (EC 3.6.1.9) (Non-canonical purine NTP pyrophosphatase) (Non-standard purine NTP pyrophosphatase) (Nucleoside-triphosphate diphosphatase) (Nucleoside-triphosphate pyrophosphatase) (NTPase)

 ITPA_ASHGO              Reviewed;         198 AA.
Q752Z9;
19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
05-DEC-2018, entry version 90.
RecName: Full=Inosine triphosphate pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_03148};
Short=ITPase {ECO:0000255|HAMAP-Rule:MF_03148};
Short=Inosine triphosphatase {ECO:0000255|HAMAP-Rule:MF_03148};
EC=3.6.1.9 {ECO:0000255|HAMAP-Rule:MF_03148};
AltName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_03148};
AltName: Full=Non-standard purine NTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_03148};
AltName: Full=Nucleoside-triphosphate diphosphatase {ECO:0000255|HAMAP-Rule:MF_03148};
AltName: Full=Nucleoside-triphosphate pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_03148};
Short=NTPase {ECO:0000255|HAMAP-Rule:MF_03148};
Name=HAM1 {ECO:0000255|HAMAP-Rule:MF_03148};
OrderedLocusNames=AFR425C;
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL
Y-1056) (Yeast) (Eremothecium gossypii).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Eremothecium.
NCBI_TaxID=284811;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
PubMed=15001715; DOI=10.1126/science.1095781;
Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
Gaffney T.D., Philippsen P.;
"The Ashbya gossypii genome as a tool for mapping the ancient
Saccharomyces cerevisiae genome.";
Science 304:304-307(2004).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
PubMed=23749448; DOI=10.1534/g3.112.002881;
Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
"Genomes of Ashbya fungi isolated from insects reveal four mating-type
loci, numerous translocations, lack of transposons, and distinct gene
duplications.";
G3 (Bethesda) 3:1225-1239(2013).
-!- FUNCTION: Pyrophosphatase that hydrolyzes non-canonical purine
nucleotides such as inosine triphosphate (ITP), deoxyinosine
triphosphate (dITP) or xanthosine 5'-triphosphate (XTP) to their
respective monophosphate derivatives. The enzyme does not
distinguish between the deoxy- and ribose forms. Probably excludes
non-canonical purines from RNA and DNA precursor pools, thus
preventing their incorporation into RNA and DNA and avoiding
chromosomal lesions. {ECO:0000255|HAMAP-Rule:MF_03148}.
-!- CATALYTIC ACTIVITY:
Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside
5'-phosphate + diphosphate + H(+); Xref=Rhea:RHEA:23996,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.9;
Evidence={ECO:0000255|HAMAP-Rule:MF_03148};
-!- CATALYTIC ACTIVITY:
Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'-
deoxyribonucleoside 5'-phosphate + diphosphate + H(+);
Xref=Rhea:RHEA:44644, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:65317;
EC=3.6.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_03148};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_03148};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000255|HAMAP-Rule:MF_03148};
Note=Binds 1 divalent metal cation per subunit; can use either
Mg(2+) or Mn(2+). {ECO:0000255|HAMAP-Rule:MF_03148};
-!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03148}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03148}.
Nucleus {ECO:0000255|HAMAP-Rule:MF_03148}.
-!- SIMILARITY: Belongs to the HAM1 NTPase family. {ECO:0000255|HAMAP-
Rule:MF_03148}.
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EMBL; AE016819; AAS53796.1; -; Genomic_DNA.
RefSeq; NP_985972.1; NM_211327.1.
ProteinModelPortal; Q752Z9; -.
SMR; Q752Z9; -.
STRING; 33169.AAS53796; -.
PRIDE; Q752Z9; -.
EnsemblFungi; AAS53796; AAS53796; AGOS_AFR425C.
GeneID; 4622245; -.
KEGG; ago:AGOS_AFR425C; -.
HOGENOM; HOG000293320; -.
InParanoid; Q752Z9; -.
KO; K01519; -.
OMA; YDPIFQP; -.
OrthoDB; EOG092C523G; -.
Proteomes; UP000000591; Chromosome VI.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0035529; F:NADH pyrophosphatase activity; IEA:UniProtKB-EC.
GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IBA:GO_Central.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
GO; GO:0009204; P:deoxyribonucleoside triphosphate catabolic process; IEA:UniProtKB-UniRule.
GO; GO:0009143; P:nucleoside triphosphate catabolic process; IBA:GO_Central.
GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
CDD; cd00515; HAM1; 1.
Gene3D; 3.90.950.10; -; 1.
HAMAP; MF_03148; HAM1_NTPase; 1.
InterPro; IPR002637; Ham1p-like.
InterPro; IPR027502; ITPase.
InterPro; IPR029001; ITPase-like_fam.
PANTHER; PTHR11067; PTHR11067; 1.
Pfam; PF01725; Ham1p_like; 1.
SUPFAM; SSF52972; SSF52972; 1.
TIGRFAMs; TIGR00042; TIGR00042; 1.
3: Inferred from homology;
Complete proteome; Cytoplasm; Hydrolase; Magnesium; Manganese;
Metal-binding; Nucleotide metabolism; Nucleotide-binding; Nucleus;
Reference proteome.
CHAIN 1 198 Inosine triphosphate pyrophosphatase.
/FTId=PRO_0000413127.
REGION 8 13 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_03148}.
REGION 70 71 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_03148}.
REGION 145 148 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_03148}.
REGION 173 174 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_03148}.
METAL 39 39 Magnesium or manganese.
{ECO:0000255|HAMAP-Rule:MF_03148}.
METAL 70 70 Magnesium or manganese.
{ECO:0000255|HAMAP-Rule:MF_03148}.
BINDING 52 52 Substrate. {ECO:0000255|HAMAP-
Rule:MF_03148}.
BINDING 168 168 Substrate. {ECO:0000255|HAMAP-
Rule:MF_03148}.
SEQUENCE 198 AA; 21130 MW; B0013E129B66506C CRC64;
MPNLVFVTGN ANKLREVRQL LGGAALPYPL VNEPLDLDEV QAASLDAIAL HKCRSAAARL
PPGTPVFVED TALCFDALGG LPGAYIKWYV QAMPLCDIAS MLDAFPAKTA RAVTTVAYCD
AAGAFHTFSG TTTGRIVPPR GPTDFGWDAI FEPAGEDKTY AEMDKDKKNA ISHRGKAFAA
FREHLCSPSQ RPPPPATA


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