IXTPA_ELUMP
ID IXTPA_ELUMP Reviewed; 197 AA.
AC B2KEA9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=dITP/XTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01405};
DE EC=3.6.1.66 {ECO:0000255|HAMAP-Rule:MF_01405};
DE AltName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01405};
DE AltName: Full=Non-standard purine NTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01405};
DE AltName: Full=Nucleoside-triphosphate diphosphatase {ECO:0000255|HAMAP-Rule:MF_01405};
DE AltName: Full=Nucleoside-triphosphate pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01405};
DE Short=NTPase {ECO:0000255|HAMAP-Rule:MF_01405};
GN OrderedLocusNames=Emin_1305;
OS Elusimicrobium minutum (strain Pei191).
OC Bacteria; Elusimicrobia; Elusimicrobia; Elusimicrobiales;
OC Elusimicrobiaceae; Elusimicrobium.
OX NCBI_TaxID=445932;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pei191;
RX PubMed=19270133; DOI=10.1128/aem.02698-08;
RA Herlemann D.P.R., Geissinger O., Ikeda-Ohtsubo W., Kunin V., Sun H.,
RA Lapidus A., Hugenholtz P., Brune A.;
RT "Genomic analysis of 'Elusimicrobium minutum,' the first cultivated
RT representative of the phylum 'Elusimicrobia' (formerly termite group 1).";
RL Appl. Environ. Microbiol. 75:2841-2849(2009).
CC -!- FUNCTION: Pyrophosphatase that catalyzes the hydrolysis of nucleoside
CC triphosphates to their monophosphate derivatives, with a high
CC preference for the non-canonical purine nucleotides XTP (xanthosine
CC triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to
CC function as a house-cleaning enzyme that removes non-canonical purine
CC nucleotides from the nucleotide pool, thus preventing their
CC incorporation into DNA/RNA and avoiding chromosomal lesions.
CC {ECO:0000255|HAMAP-Rule:MF_01405}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + XTP = diphosphate + H(+) + XMP; Xref=Rhea:RHEA:28610,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57464, ChEBI:CHEBI:61314; EC=3.6.1.66;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01405};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dITP + H2O = dIMP + diphosphate + H(+); Xref=Rhea:RHEA:28342,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:61194, ChEBI:CHEBI:61382; EC=3.6.1.66;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01405};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + ITP = diphosphate + H(+) + IMP; Xref=Rhea:RHEA:29399,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58053, ChEBI:CHEBI:61402; EC=3.6.1.66;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01405};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01405};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01405};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01405}.
CC -!- SIMILARITY: Belongs to the HAM1 NTPase family. {ECO:0000255|HAMAP-
CC Rule:MF_01405}.
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DR EMBL; CP001055; ACC98855.1; -; Genomic_DNA.
DR RefSeq; WP_012415470.1; NC_010644.1.
DR AlphaFoldDB; B2KEA9; -.
DR SMR; B2KEA9; -.
DR STRING; 445932.Emin_1305; -.
DR EnsemblBacteria; ACC98855; ACC98855; Emin_1305.
DR KEGG; emi:Emin_1305; -.
DR HOGENOM; CLU_082080_0_2_0; -.
DR OMA; DCFADDT; -.
DR OrthoDB; 1824064at2; -.
DR Proteomes; UP000001029; Chromosome.
DR GO; GO:0035870; F:dITP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0036220; F:ITP diphosphatase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0036222; F:XTP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009146; P:purine nucleoside triphosphate catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd00515; HAM1; 1.
DR Gene3D; 3.90.950.10; -; 1.
DR HAMAP; MF_01405; Non_canon_purine_NTPase; 1.
DR InterPro; IPR020922; dITP/XTP_pyrophosphatase.
DR InterPro; IPR002637; Ham1p-like.
DR InterPro; IPR029001; ITPase-like_fam.
DR PANTHER; PTHR11067; PTHR11067; 1.
DR Pfam; PF01725; Ham1p_like; 1.
DR SUPFAM; SSF52972; SSF52972; 1.
DR TIGRFAMs; TIGR00042; TIGR00042; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..197
FT /note="dITP/XTP pyrophosphatase"
FT /id="PRO_1000145489"
FT ACT_SITE 73
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405"
FT BINDING 7..12
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405"
FT BINDING 44
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405"
FT BINDING 73
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405"
FT BINDING 74
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405"
FT BINDING 156..159
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405"
FT BINDING 184..185
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405"
SQ SEQUENCE 197 AA; 21651 MW; 0696F013DDF4E9D1 CRC64;
MKILLATGNE QKAKELKCIL PKNIGNKEIE YLTLGDFPDL RMPEETGKTL EENAILKARE
AARQAGIAAL ADDTGLEVDA LNGEPGVRSA RYAGEYCDPD ENNRKLLDSL DGLFLGQRTA
RFKTVACLAT PEGEYELAEG VLGGLIGFGY RGENGFGYDP LFIVKGKSKT LAELTLDEKN
KISHRRKAFE KISKKIK
