IXTPA_GEOKA
ID IXTPA_GEOKA Reviewed; 204 AA.
AC Q5KWI6;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=GK2665;
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(2004).
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; BA000043; BAD76950.1; -; Genomic_DNA.
DR RefSeq; WP_011232140.1; NC_006510.1.
DR AlphaFoldDB; Q5KWI6; -.
DR SMR; Q5KWI6; -.
DR STRING; 235909.GK2665; -.
DR EnsemblBacteria; BAD76950; BAD76950; GK2665.
DR KEGG; gka:GK2665; -.
DR eggNOG; COG0127; Bacteria.
DR HOGENOM; CLU_082080_0_2_9; -.
DR OMA; DCFADDT; -.
DR Proteomes; UP000001172; 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..204
FT /note="dITP/XTP pyrophosphatase"
FT /id="PRO_0000178169"
FT ACT_SITE 70
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405"
FT BINDING 8..13
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405"
FT BINDING 70
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405"
FT BINDING 71
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405"
FT BINDING 153..156
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405"
FT BINDING 181..182
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405"
SQ SEQUENCE 204 AA; 22016 MW; 63F14481C9892B75 CRC64;
MKEIVIATKN AGKVREFAAL FAKRGVEVKS LLDFPDAPDV AETGSTFAEN AVLKAEAASR
RLKRPVIADD SGLVVDALGG RPGVHSARYA GEDKNDARNI AKLLRELDGV PMEQRTARFH
CALAVAIPGR PTAVVEATCD GYIAEAPRGE GGFGYDPVFY LPERGKTMAE LAPEEKNQIS
HRAKALTKLD EQWEEIVGGK GRTE
