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IXTPA_MYCTO
ID   IXTPA_MYCTO             Reviewed;         204 AA.
AC   P9WMR6; L0T939; P64307; Q10649;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 39.
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=MT1382;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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; AE000516; AAK45647.1; -; Genomic_DNA.
DR   PIR; D70739; D70739.
DR   RefSeq; WP_003406931.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WMR6; -.
DR   SMR; P9WMR6; -.
DR   EnsemblBacteria; AAK45647; AAK45647; MT1382.
DR   GeneID; 45425319; -.
DR   KEGG; mtc:MT1382; -.
DR   PATRIC; fig|83331.31.peg.1490; -.
DR   HOGENOM; CLU_082080_0_1_11; -.
DR   Proteomes; UP000001020; 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.
FT   CHAIN           1..204
FT                   /note="dITP/XTP pyrophosphatase"
FT                   /id="PRO_0000427255"
FT   ACT_SITE        76
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01405"
FT   BINDING         11..16
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01405"
FT   BINDING         76
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01405"
FT   BINDING         77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01405"
FT   BINDING         158..161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01405"
FT   BINDING         181
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01405"
FT   BINDING         186..187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01405"
SQ   SEQUENCE   204 AA;  21016 MW;  879DF0B08A5CCAEE CRC64;
     MALVTKLLVA SRNRKKLAEL RRVLDGAGLS GLTLLSLGDV SPLPETPETG VTFEDNALAK
     ARDAFSATGL ASVADDSGLE VAALGGMPGV LSARWSGRYG DDAANTALLL AQLCDVPDER
     RGAAFVSACA LVSGSGEVVV RGEWPGTIAR EPRGDGGFGY DPVFVPYGDD RTAAQLSPAE
     KDAVSHRGRA LALLLPALRS LATG
 
 
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