ID D5WUL4_KYRT2 Unreviewed; 207 AA.
AC D5WUL4;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=dITP/XTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405};
DE EC=3.6.1.66 {ECO:0000256|HAMAP-Rule:MF_01405};
DE AltName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405};
DE AltName: Full=Non-standard purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405};
DE AltName: Full=Nucleoside-triphosphate diphosphatase {ECO:0000256|HAMAP-Rule:MF_01405};
DE AltName: Full=Nucleoside-triphosphate pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405};
DE Short=NTPase {ECO:0000256|HAMAP-Rule:MF_01405};
GN OrderedLocusNames=Btus_0641 {ECO:0000313|EMBL:ADG05404.1};
OS Kyrpidia tusciae (strain DSM 2912 / NBRC 15312 / T2) (Bacillus tusciae).
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae; Kyrpidia.
OX NCBI_TaxID=562970 {ECO:0000313|EMBL:ADG05404.1, ECO:0000313|Proteomes:UP000002368};
RN [1] {ECO:0000313|Proteomes:UP000002368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2912 / NBRC 15312 / T2 {ECO:0000313|Proteomes:UP000002368};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Ovchinnikova G., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F.,
RA Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA Wu D., Pukall R., Schneider S., Wahrenburg C., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Bacillus tusciae DSM 2912.";
RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADG05404.1, ECO:0000313|Proteomes:UP000002368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2912 / NBRC 15312 / T2 {ECO:0000313|Proteomes:UP000002368};
RX PubMed=22180816; DOI=10.4056/sigs.2144922;
RA Klenk H.P., Lapidus A., Chertkov O., Copeland A., Del Rio T.G., Nolan M.,
RA Lucas S., Chen F., Tice H., Cheng J.F., Han C., Bruce D., Goodwin L.,
RA Pitluck S., Pati A., Ivanova N., Mavromatis K., Daum C., Chen A.,
RA Palaniappan K., Chang Y.J., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA Rohde M., Abt B., Pukall R., Goker M., Bristow J., Markowitz V.,
RA Hugenholtz P., Eisen J.A.;
RT "Complete genome sequence of the thermophilic, hydrogen-oxidizing Bacillus
RT tusciae type strain (T2) and reclassification in the new genus, Kyrpidia
RT gen. nov. as Kyrpidia tusciae comb. nov. and emendation of the family
RT Alicyclobacillaceae da Costa and Rainey, 2010.";
RL Stand. Genomic Sci. 5:121-134(2011).
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:0000256|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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01405};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01405};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01405};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01405}.
CC -!- SIMILARITY: Belongs to the HAM1 NTPase family.
CC {ECO:0000256|ARBA:ARBA00008023, ECO:0000256|HAMAP-Rule:MF_01405,
CC ECO:0000256|RuleBase:RU003781}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01405}.
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DR EMBL; CP002017; ADG05404.1; -; Genomic_DNA.
DR AlphaFoldDB; D5WUL4; -.
DR STRING; 562970.Btus_0641; -.
DR KEGG; bts:Btus_0641; -.
DR eggNOG; COG0127; Bacteria.
DR HOGENOM; CLU_082080_0_2_9; -.
DR Proteomes; UP000002368; Chromosome.
DR GO; GO:0035870; F:dITP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0036220; F:ITP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:InterPro.
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; IPR029001; ITPase-like_fam.
DR InterPro; IPR002637; RdgB/HAM1.
DR NCBIfam; TIGR00042; RdgB/HAM1 family non-canonical purine NTP pyrophosphatase; 1.
DR PANTHER; PTHR11067:SF9; INOSINE TRIPHOSPHATE PYROPHOSPHATASE; 1.
DR PANTHER; PTHR11067; INOSINE TRIPHOSPHATE PYROPHOSPHATASE/HAM1 PROTEIN; 1.
DR Pfam; PF01725; Ham1p_like; 1.
DR SUPFAM; SSF52972; ITPase-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01405};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01405};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01405}; Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_01405};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01405}.
FT ACT_SITE 70
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT BINDING 8..13
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT BINDING 70
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT BINDING 71
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT BINDING 154..157
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
FT BINDING 182..183
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01405"
SQ SEQUENCE 207 AA; 22490 MW; 07D7CE64F2BDD510 CRC64;
MYTVVLATHN KGKVREFREM LRPLGWDVFP LSAFPGYVPP PETGATFCEN ALIKARDAAE
RLGLPALADD SGLEVEALEG RPGVFSARFA GPGATDEENN RLLLAELERS PAPPPWAARF
VCCLAWVEPS GETHTFHGET RGWILAQPRG SGGFGYDPLF WSPELQQTFG EAPPEAKNRV
SHRKRALEAL VQALSRPEKG APGASSV
//
