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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)

 V6XUM0_BIFLN            Unreviewed;       252 AA.
V6XUM0;
19-FEB-2014, integrated into UniProtKB/TrEMBL.
19-FEB-2014, sequence version 1.
25-OCT-2017, entry version 29.
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=BLONG_0355 {ECO:0000313|EMBL:ESV32942.1};
Bifidobacterium longum E18.
Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
Bifidobacterium.
NCBI_TaxID=1322347 {ECO:0000313|EMBL:ESV32942.1, ECO:0000313|Proteomes:UP000018321};
[1] {ECO:0000313|Proteomes:UP000018321}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=24356845;
Zhurina D., Dudnik A., Waidmann M.S., Grimm V., Westermann C.,
Breitinger K.J., Yuan J., van Sinderen D., Riedel C.U.;
"High-Quality Draft Genome Sequence of Bifidobacterium longum E18,
Isolated from a Healthy Adult.";
Genome Announc. 1:e01084-13(2013).
-!- 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|SAAS:SAAS00730348}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01405}.
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EMBL; CM002287; ESV32942.1; -; Genomic_DNA.
RefSeq; WP_007051401.1; NZ_CM002287.1.
ProteinModelPortal; V6XUM0; -.
SMR; V6XUM0; -.
EnsemblBacteria; ESV32942; ESV32942; BLONG_0355.
PATRIC; fig|1322347.4.peg.349; -.
Proteomes; UP000018321; Chromosome.
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; 2.
Pfam; PF01725; Ham1p_like; 1.
SUPFAM; SSF52972; SSF52972; 2.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000018321};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_01405,
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 7 12 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01405}.
REGION 193 196 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01405}.
REGION 235 236 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01405}.
ACT_SITE 74 74 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_01405}.
METAL 74 74 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01405}.
BINDING 75 75 Substrate; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01405}.
BINDING 230 230 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01405}.
SEQUENCE 252 AA; 26418 MW; 9ADE11FC052CF3F0 CRC64;
MQIVVATHNE GKLVEIRRIL EEDLGADAEN IELVSAGSLH LPDPVETGVT FQENALLKAR
AVAIRTGLPA VADDSGLIVD VMGNAPGILS ARWAGAHGHD KANNALLLAQ IEDIPDDKRT
ARFRCAAALV VPDTETGADV TGGVAADGIT VHTTAADGSP APVHARYAIK SETVELGDMP
GRIIREARGV HGFGYDPLFV PDDQPAGRVS TEPDHEGEPL TSAEMTPAEK NAISHRGKAL
KALVPAIEAL LH


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