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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)

 G3BAV3_CANTC            Unreviewed;       192 AA.
G3BAV3;
16-NOV-2011, integrated into UniProtKB/TrEMBL.
16-NOV-2011, sequence version 1.
13-FEB-2019, entry version 43.
RecName: Full=Inosine triphosphate pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_03148};
Short=ITPase {ECO:0000256|HAMAP-Rule:MF_03148};
Short=Inosine triphosphatase {ECO:0000256|HAMAP-Rule:MF_03148};
EC=3.6.1.9 {ECO:0000256|HAMAP-Rule:MF_03148};
AltName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_03148};
AltName: Full=Non-standard purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_03148};
AltName: Full=Nucleoside-triphosphate diphosphatase {ECO:0000256|HAMAP-Rule:MF_03148};
AltName: Full=Nucleoside-triphosphate pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_03148};
Short=NTPase {ECO:0000256|HAMAP-Rule:MF_03148};
Name=HAM1 {ECO:0000256|HAMAP-Rule:MF_03148};
ORFNames=CANTEDRAFT_114925 {ECO:0000313|EMBL:EGV62528.1};
Candida tenuis (strain ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 /
NBRC 10315 / NRRL Y-1498 / VKM Y-70) (Yeast) (Yamadazyma tenuis).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Yamadazyma.
NCBI_TaxID=590646 {ECO:0000313|Proteomes:UP000000707};
[1] {ECO:0000313|EMBL:EGV62528.1, ECO:0000313|Proteomes:UP000000707}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 10573 {ECO:0000313|EMBL:EGV62528.1}, and
ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC 10315 / NRRL
Y-1498 / VKM Y-70 {ECO:0000313|Proteomes:UP000000707};
PubMed=21788494; DOI=10.1073/pnas.1103039108;
Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A.,
LaButti K.M., Sun H., Clum A., Pangilinan J.L., Lindquist E.A.,
Lucas S., Lapidus A., Jin M., Gunawan C., Balan V., Dale B.E.,
Jeffries T.W., Zinkel R., Barry K.W., Grigoriev I.V., Gasch A.P.;
"Comparative genomics of xylose-fermenting fungi for enhanced biofuel
production.";
Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
-!- 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:0000256|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:0000256|HAMAP-Rule:MF_03148,
ECO:0000256|SAAS:SAAS01117280};
-!- 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:0000256|HAMAP-Rule:MF_03148,
ECO:0000256|SAAS:SAAS01117281};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_03148};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000256|HAMAP-Rule:MF_03148};
Note=Binds 1 divalent metal cation per subunit; can use either
Mg(2+) or Mn(2+). {ECO:0000256|HAMAP-Rule:MF_03148};
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03148,
ECO:0000256|SAAS:SAAS00721538}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03148}.
Nucleus {ECO:0000256|HAMAP-Rule:MF_03148}.
-!- SIMILARITY: Belongs to the HAM1 NTPase family. {ECO:0000256|HAMAP-
Rule:MF_03148, ECO:0000256|RuleBase:RU003781,
ECO:0000256|SAAS:SAAS00721539}.
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EMBL; GL996527; EGV62528.1; -; Genomic_DNA.
EMBL; GL996527; EGV62529.1; -; Genomic_DNA.
RefSeq; XP_006688698.1; XM_006688635.1.
RefSeq; XP_006688699.1; XM_006688636.1.
EnsemblFungi; EGV62528; EGV62528; CANTEDRAFT_114925.
EnsemblFungi; EGV62529; EGV62529; CANTEDRAFT_114925.
GeneID; 18247636; -.
KEGG; cten:CANTEDRAFT_114925; -.
KO; K01519; -.
OrthoDB; 1298391at2759; -.
Proteomes; UP000000707; Unassembled WGS sequence.
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; IEA:UniProtKB-UniRule.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
GO; GO:0009204; P:deoxyribonucleoside triphosphate catabolic process; IEA:UniProtKB-UniRule.
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;
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000000707};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03148,
ECO:0000256|SAAS:SAAS00721512};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_03148,
ECO:0000256|RuleBase:RU003781, ECO:0000256|SAAS:SAAS00721541};
Magnesium {ECO:0000256|HAMAP-Rule:MF_03148,
ECO:0000256|SAAS:SAAS00721547};
Manganese {ECO:0000256|HAMAP-Rule:MF_03148};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_03148,
ECO:0000256|SAAS:SAAS00721543};
Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_03148,
ECO:0000256|SAAS:SAAS00721522};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03148,
ECO:0000256|SAAS:SAAS00721527};
Nucleus {ECO:0000256|HAMAP-Rule:MF_03148};
Reference proteome {ECO:0000313|Proteomes:UP000000707}.
REGION 8 13 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_03148}.
REGION 73 74 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_03148}.
REGION 149 152 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_03148}.
REGION 177 178 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_03148}.
COILED 43 63 {ECO:0000256|SAM:Coils}.
METAL 45 45 Magnesium or manganese.
{ECO:0000256|HAMAP-Rule:MF_03148}.
METAL 73 73 Magnesium or manganese.
{ECO:0000256|HAMAP-Rule:MF_03148}.
BINDING 57 57 Substrate. {ECO:0000256|HAMAP-
Rule:MF_03148}.
BINDING 172 172 Substrate. {ECO:0000256|HAMAP-
Rule:MF_03148}.
SEQUENCE 192 AA; 21150 MW; D11B4FB42ADF6CBD CRC64;
MSTITFVTGN KNKLKEVVAI LAGETDGKSN VGKFTIVNAA LDLDEYQGTV EEVTARKAKT
AAELINGPVM VEDTCLGYDA MKGLPGPYIK WFVNSVGLTG LVDMLYKFED KGAKAICTFG
YCEGPGKEVR LFQGVTEGKI VDSRGHTNFG WDSIFEPNGF NQTYAEMDKS VKNTISHRFK
ALDKLREFLL QQ


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Pathways :
WP1709: Thiamine metabolism
WP1694: Pyrimidine metabolism
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP2341: vitamin B1 (thiamin) biosynthesis and salvage pathway
WP1693: Purine metabolism
WP203: De Novo Biosynthesis of Purine Nucleotides
WP2184: Purine metabolism
WP2185: Purine metabolism
WP416: Superpathway of Histidine, Purine, and Pyrimidine
WP463: Purine Fermentation
WP566: canonical wnt - zebrafish

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[Itpa] 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)
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Bibliography :
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