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Inosine triphosphate pyrophosphatase (ITPase) (Inosine triphosphatase) (EC 3.6.1.9) (Hydroxylaminopurine sensitivity protein 1) (Non-canonical purine NTP pyrophosphatase) (Non-standard purine NTP pyrophosphatase) (Nucleoside-triphosphate diphosphatase) (Nucleoside-triphosphate pyrophosphatase) (NTPase)

 ITPA_YEAST              Reviewed;         197 AA.
P47119; D6VWP0;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
25-OCT-2017, entry version 138.
RecName: Full=Inosine triphosphate pyrophosphatase {ECO:0000270|HAMAP-Rule:MF_03148};
Short=ITPase {ECO:0000270|HAMAP-Rule:MF_03148};
Short=Inosine triphosphatase {ECO:0000270|HAMAP-Rule:MF_03148};
EC=3.6.1.9 {ECO:0000269|PubMed:17090528, ECO:0000270|HAMAP-Rule:MF_03148};
AltName: Full=Hydroxylaminopurine sensitivity protein 1;
AltName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000270|HAMAP-Rule:MF_03148};
AltName: Full=Non-standard purine NTP pyrophosphatase {ECO:0000270|HAMAP-Rule:MF_03148};
AltName: Full=Nucleoside-triphosphate diphosphatase {ECO:0000270|HAMAP-Rule:MF_03148};
AltName: Full=Nucleoside-triphosphate pyrophosphatase {ECO:0000270|HAMAP-Rule:MF_03148};
Short=NTPase {ECO:0000270|HAMAP-Rule:MF_03148};
Name=HAM1 {ECO:0000270|HAMAP-Rule:MF_03148};
OrderedLocusNames=YJR069C; ORFNames=J1811;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8789257;
DOI=10.1002/(SICI)1097-0061(199601)12:1<17::AID-YEA875>3.0.CO;2-I;
Noskov V.N., Staak K., Shcherbakova P.V., Kozmin S.G., Negishi K.,
Ono B.-C., Hayatsu H., Pavlov Y.I.;
"HAM1, the gene controlling 6-N-hydroxylaminopurine sensitivity and
mutagenesis in the yeast Saccharomyces cerevisiae.";
Yeast 12:17-29(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8840504;
DOI=10.1002/(SICI)1097-0061(199607)12:9<869::AID-YEA964>3.0.CO;2-1;
Huang M.-E., Manus V., Chuat J.-C., Galibert F.;
"Analysis of a 62 kb DNA sequence of chromosome X reveals 36 open
reading frames and a gene cluster with a counterpart on chromosome
XI.";
Yeast 12:869-875(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8641269;
Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N.,
Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H.,
Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A.,
Hennemann A., Herbert C.J., Heumann K., Hilger F., Hollenberg C.P.,
Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L.,
Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V.,
Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M.,
Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W.,
Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M.,
Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A.,
Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M.,
Zollner A., Karpfinger-Hartl L.;
"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
X.";
EMBO J. 15:2031-2049(1996).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[6]
FUNCTION.
PubMed=9918490;
Kozmin S.G., Leroy P., Pavlov Y.I.;
"Overexpression of the yeast HAM1 gene prevents 6-N-
hydroxylaminopurine mutagenesis in Escherichia coli.";
Acta Biochim. Pol. 45:645-652(1998).
[7]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[8]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[9]
FUNCTION.
PubMed=17899088; DOI=10.1007/s00294-007-0152-z;
Takayama S., Fujii M., Kurosawa A., Adachi N., Ayusawa D.;
"Overexpression of HAM1 gene detoxifies 5-bromodeoxyuridine in the
yeast Saccharomyces cerevisiae.";
Curr. Genet. 52:203-211(2007).
[10]
SUBSTRATE SPECIFICITY, FUNCTION, CATALYTIC ACTIVITY, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=17090528; DOI=10.1074/jbc.M608708200;
Burgis N.E., Cunningham R.P.;
"Substrate specificity of RdgB protein, a deoxyribonucleoside
triphosphate pyrophosphohydrolase.";
J. Biol. Chem. 282:3531-3538(2007).
-!- FUNCTION: Pyrophosphatase that hydrolyzes the non-canonical purine
nucleotides inosine triphosphate (ITP), deoxyinosine triphosphate
(dITP) as well as 2'-deoxy-N-6-hydroxylaminopurine triposphate
(dHAPTP) and 5-bromodeoxyuridine 5'-triphosphate (BrdUTP) to their
respective monophosphate derivatives. Xanthosine 5'-triphosphate
(XTP) is also a potential substrate. 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:0000269|PubMed:17090528,
ECO:0000269|PubMed:17899088, ECO:0000269|PubMed:9918490,
ECO:0000270|HAMAP-Rule:MF_03148}.
-!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a
nucleotide + diphosphate. {ECO:0000269|PubMed:17090528,
ECO:0000270|HAMAP-Rule:MF_03148}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000270|HAMAP-Rule:MF_03148};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000270|HAMAP-Rule:MF_03148};
Note=Binds 1 divalent metal cation per subunit; can use either
Mg(2+) or Mn(2+). {ECO:0000270|HAMAP-Rule:MF_03148};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=13.4 uM for dITP {ECO:0000269|PubMed:17090528};
KM=26.9 uM for dHAPTP {ECO:0000269|PubMed:17090528};
KM=722 uM for dGTP {ECO:0000269|PubMed:17090528};
Note=Vmax values are similar for dITP, dHAPTP and dGTP.;
-!- SUBUNIT: Homodimer. {ECO:0000270|HAMAP-Rule:MF_03148}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
ECO:0000270|HAMAP-Rule:MF_03148}. Nucleus
{ECO:0000269|PubMed:14562095, ECO:0000270|HAMAP-Rule:MF_03148}.
-!- MISCELLANEOUS: Present with 3490 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the HAM1 NTPase family. {ECO:0000270|HAMAP-
Rule:MF_03148}.
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EMBL; Z49569; CAA89597.1; -; Genomic_DNA.
EMBL; L47993; AAB39295.1; -; Genomic_DNA.
EMBL; AY557897; AAS56223.1; -; Genomic_DNA.
EMBL; BK006943; DAA08856.1; -; Genomic_DNA.
PIR; S57088; S57088.
RefSeq; NP_012603.1; NM_001181727.1.
ProteinModelPortal; P47119; -.
SMR; P47119; -.
BioGrid; 33826; 48.
DIP; DIP-5491N; -.
IntAct; P47119; 5.
MINT; MINT-476946; -.
STRING; 4932.YJR069C; -.
iPTMnet; P47119; -.
MaxQB; P47119; -.
PRIDE; P47119; -.
EnsemblFungi; YJR069C; YJR069C; YJR069C.
GeneID; 853532; -.
KEGG; sce:YJR069C; -.
EuPathDB; FungiDB:YJR069C; -.
SGD; S000003830; HAM1.
GeneTree; ENSGT00390000015399; -.
HOGENOM; HOG000293320; -.
InParanoid; P47119; -.
KO; K01519; -.
OMA; YDPIFQP; -.
OrthoDB; EOG092C523G; -.
BioCyc; YEAST:G3O-31702-MONOMER; -.
Reactome; R-SCE-74259; Purine catabolism.
PRO; PR:P47119; -.
Proteomes; UP000002311; Chromosome X.
GO; GO:0005737; C:cytoplasm; RCA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; RCA:UniProtKB-SubCell.
GO; GO:0008828; F:dATP pyrophosphohydrolase activity; HTP:SGD.
GO; GO:0047840; F:dCTP diphosphatase activity; HTP:SGD.
GO; GO:0036217; F:dGTP diphosphatase activity; HTP:SGD.
GO; GO:0035870; F:dITP diphosphatase activity; HTP:SGD.
GO; GO:0036218; F:dTTP diphosphatase activity; HTP:SGD.
GO; GO:0004170; F:dUTP diphosphatase activity; HTP:SGD.
GO; GO:0036219; F:GTP diphosphatase activity; HTP:SGD.
GO; GO:0036220; F:ITP diphosphatase activity; HTP:SGD.
GO; GO:0046872; F:metal ion binding; RCA:UniProtKB-KW.
GO; GO:0035529; F:NADH pyrophosphatase activity; RCA:UniProtKB-EC.
GO; GO:0000166; F:nucleotide binding; RCA:UniProtKB-KW.
GO; GO:0036221; F:UTP diphosphatase activity; HTP:SGD.
GO; GO:0036222; F:XTP diphosphatase activity; HTP:SGD.
GO; GO:0009117; P:nucleotide metabolic process; RCA:UniProtKB-KW.
GO; GO:0009217; P:purine deoxyribonucleoside triphosphate catabolic process; HTP:SGD.
GO; GO:0009213; P:pyrimidine deoxyribonucleoside triphosphate catabolic process; HTP:SGD.
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.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Hydrolase; Magnesium; Manganese;
Metal-binding; Nucleotide metabolism; Nucleotide-binding; Nucleus;
Reference proteome.
CHAIN 1 197 Inosine triphosphate pyrophosphatase.
/FTId=PRO_0000178279.
REGION 10 15 Substrate binding. {ECO:0000270|HAMAP-
Rule:MF_03148}.
REGION 76 77 Substrate binding. {ECO:0000270|HAMAP-
Rule:MF_03148}.
REGION 151 154 Substrate binding. {ECO:0000270|HAMAP-
Rule:MF_03148}.
REGION 180 181 Substrate binding. {ECO:0000270|HAMAP-
Rule:MF_03148}.
METAL 45 45 Magnesium or manganese.
{ECO:0000270|HAMAP-Rule:MF_03148}.
METAL 76 76 Magnesium or manganese.
{ECO:0000270|HAMAP-Rule:MF_03148}.
BINDING 58 58 Substrate. {ECO:0000270|HAMAP-
Rule:MF_03148}.
BINDING 175 175 Substrate. {ECO:0000270|HAMAP-
Rule:MF_03148}.
SEQUENCE 197 AA; 22093 MW; 1C7AA19465467C07 CRC64;
MSNNEIVFVT GNANKLKEVQ SILTQEVDNN NKTIHLINEA LDLEELQDTD LNAIALAKGK
QAVAALGKGK PVFVEDTALR FDEFNGLPGA YIKWFLKSMG LEKIVKMLEP FENKNAEAVT
TICFADSRGE YHFFQGITRG KIVPSRGPTT FGWDSIFEPF DSHGLTYAEM SKDAKNAISH
RGKAFAQFKE YLYQNDF


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