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dITP/XTP pyrophosphatase (EC 3.6.1.66) (Non-canonical purine NTP pyrophosphatase) (Non-standard purine NTP pyrophosphatase) (Nucleoside-triphosphate diphosphatase) (Nucleoside-triphosphate pyrophosphatase) (NTPase)

 U1S5L7_9ACTO            Unreviewed;       205 AA.
U1S5L7;
13-NOV-2013, integrated into UniProtKB/TrEMBL.
13-NOV-2013, sequence version 1.
27-SEP-2017, entry version 26.
RecName: Full=dITP/XTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405};
EC=3.6.1.66 {ECO:0000256|HAMAP-Rule:MF_01405};
AltName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405};
AltName: Full=Non-standard purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405};
AltName: Full=Nucleoside-triphosphate diphosphatase {ECO:0000256|HAMAP-Rule:MF_01405};
AltName: Full=Nucleoside-triphosphate pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405};
Short=NTPase {ECO:0000256|HAMAP-Rule:MF_01405};
ORFNames=HMPREF1550_02597 {ECO:0000313|EMBL:ERH25927.1};
Actinomyces sp. oral taxon 877 str. F0543.
Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae;
Actinomyces.
NCBI_TaxID=1227264 {ECO:0000313|EMBL:ERH25927.1, ECO:0000313|Proteomes:UP000016532};
[1] {ECO:0000313|EMBL:ERH25927.1, ECO:0000313|Proteomes:UP000016532}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=F0543 {ECO:0000313|EMBL:ERH25927.1,
ECO:0000313|Proteomes:UP000016532};
Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R.,
Courtney L., Fronick C., O'Laughlin M., Godfrey J., Wilson R.M.,
Miner T., Farmer C., Delehaunty K., Cordes M., Minx P., Tomlinson C.,
Chen J., Wollam A., Pepin K.H., Bhonagiri V., Zhang X., Warren W.,
Mitreva M., Mardis E.R., Wilson R.K.;
Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Pyrophosphatase that catalyzes the hydrolysis of
nucleoside triphosphates to their monophosphate derivatives, with
a high preference for the non-canonical purine nucleotides XTP
(xanthosine triphosphate), dITP (deoxyinosine triphosphate) and
ITP. Seems to function as a house-cleaning enzyme that removes
non-canonical purine nucleotides from the nucleotide pool, thus
preventing their incorporation into DNA/RNA and avoiding
chromosomal lesions. {ECO:0000256|HAMAP-Rule:MF_01405,
ECO:0000256|SAAS:SAAS00805977}.
-!- CATALYTIC ACTIVITY: ITP + H(2)O = IMP + diphosphate.
{ECO:0000256|HAMAP-Rule:MF_01405, ECO:0000256|SAAS:SAAS00805978}.
-!- CATALYTIC ACTIVITY: XTP + H(2)O = XMP + diphosphate.
{ECO:0000256|HAMAP-Rule:MF_01405, ECO:0000256|SAAS:SAAS00805983}.
-!- CATALYTIC ACTIVITY: dITP + H(2)O = dIMP + diphosphate.
{ECO:0000256|HAMAP-Rule:MF_01405, ECO:0000256|SAAS:SAAS00805979}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_01405};
Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
Rule:MF_01405};
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01405,
ECO:0000256|SAAS:SAAS00730484}.
-!- SIMILARITY: Belongs to the HAM1 NTPase family. {ECO:0000256|HAMAP-
Rule:MF_01405, ECO:0000256|RuleBase:RU003781,
ECO:0000256|SAAS:SAAS00730348}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01405}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:ERH25927.1}.
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EMBL; AWSG01000248; ERH25927.1; -; Genomic_DNA.
RefSeq; WP_021613575.1; NZ_KE952419.1.
EnsemblBacteria; ERH25927; ERH25927; HMPREF1550_02597.
PATRIC; fig|1227264.3.peg.2199; -.
OrthoDB; POG091H02BP; -.
Proteomes; UP000016532; Unassembled WGS sequence.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IEA:UniProtKB-UniRule.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
GO; GO:0009146; P:purine nucleoside triphosphate catabolic process; IEA:UniProtKB-UniRule.
CDD; cd00515; HAM1; 1.
Gene3D; 3.90.950.10; -; 1.
HAMAP; MF_01405; Non_canon_purine_NTPase; 1.
InterPro; IPR020922; dITP/XTP_pyrophosphatase.
InterPro; IPR002637; Ham1p-like.
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 {ECO:0000313|Proteomes:UP000016532};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_01405,
ECO:0000256|RuleBase:RU003781, ECO:0000256|SAAS:SAAS00730407};
Magnesium {ECO:0000256|HAMAP-Rule:MF_01405,
ECO:0000256|SAAS:SAAS00730390};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01405,
ECO:0000256|SAAS:SAAS00730432};
Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_01405,
ECO:0000256|SAAS:SAAS00730340};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01405,
ECO:0000256|SAAS:SAAS00730332}.
REGION 10 15 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01405}.
REGION 159 162 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01405}.
REGION 187 188 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01405}.
ACT_SITE 76 76 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_01405}.
METAL 76 76 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01405}.
BINDING 77 77 Substrate; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01405}.
BINDING 182 182 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01405}.
SEQUENCE 205 AA; 21725 MW; BBEC284191C27B05 CRC64;
MSAPRLVFAT GNAHKISELE AILAPAWEGF DSPMIARMSD FDAEAPVEDG ASFEENALIK
ARHLAALTGL AALADDSGLT VDVMGGAPGI FSARWCGRHG DDAANLDLLL AQLADVPDAL
RSAAFVSAAV LVLPDGREFV ERGEVRGRLL RERRGGGGFG YDPVFVPDGH ALTTAQMSAE
QKNAISHRGR AFRALVPAVI DYLRS


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