IXTPA_THEMA
ID IXTPA_THEMA Reviewed; 196 AA.
AC Q9WY06;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=TM_0159;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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; AE000512; AAD35252.1; -; Genomic_DNA.
DR PIR; E72410; E72410.
DR RefSeq; NP_227974.1; NC_000853.1.
DR RefSeq; WP_004082779.1; NZ_CP011107.1.
DR PDB; 1VP2; X-ray; 1.78 A; A/B=1-196.
DR PDB; 3S86; X-ray; 2.15 A; A/B/C/D=1-196.
DR PDBsum; 1VP2; -.
DR PDBsum; 3S86; -.
DR AlphaFoldDB; Q9WY06; -.
DR SMR; Q9WY06; -.
DR STRING; 243274.THEMA_04005; -.
DR EnsemblBacteria; AAD35252; AAD35252; TM_0159.
DR KEGG; tma:TM0159; -.
DR eggNOG; COG0127; Bacteria.
DR InParanoid; Q9WY06; -.
DR OMA; DCFADDT; -.
DR OrthoDB; 1824064at2; -.
DR BRENDA; 3.6.1.66; 6331.
DR EvolutionaryTrace; Q9WY06; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0047429; F:nucleoside-triphosphate diphosphatase activity; IBA:GO_Central.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0036222; F:XTP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0009143; P:nucleoside triphosphate catabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..196
FT /note="dITP/XTP pyrophosphatase"
FT /id="PRO_0000178252"
FT ACT_SITE 68
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405"
FT BINDING 10..15
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405"
FT BINDING 68
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405"
FT BINDING 148..151
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405"
FT BINDING 175..176
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01405"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:1VP2"
FT HELIX 13..20
FT /evidence="ECO:0007829|PDB:1VP2"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:1VP2"
FT HELIX 45..60
FT /evidence="ECO:0007829|PDB:1VP2"
FT STRAND 64..73
FT /evidence="ECO:0007829|PDB:1VP2"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:1VP2"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:1VP2"
FT TURN 84..90
FT /evidence="ECO:0007829|PDB:1VP2"
FT HELIX 93..103
FT /evidence="ECO:0007829|PDB:1VP2"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:1VP2"
FT STRAND 110..121
FT /evidence="ECO:0007829|PDB:1VP2"
FT TURN 122..125
FT /evidence="ECO:0007829|PDB:1VP2"
FT STRAND 126..138
FT /evidence="ECO:0007829|PDB:1VP2"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:1VP2"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:1VP2"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:1VP2"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:1VP2"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:1VP2"
FT HELIX 175..190
FT /evidence="ECO:0007829|PDB:1VP2"
SQ SEQUENCE 196 AA; 22338 MW; 6C6E4D11901F38A8 CRC64;
MKKLTVYLAT TNPHKVEEIK MIAPEWMEIL PSPEKIEVVE DGETFLENSV KKAVVYGKKL
KHPVMADDSG LVIYSLGGFP GVMSARFMEE HSYKEKMRTI LKMLEGKDRR AAFVCSATFF
DPVENTLISV EDRVEGRIAN EIRGTGGFGY DPFFIPDGYD KTFGEIPHLK EKISHRSKAF
RKLFSVLEKI LESENR
