(data stored in ACNUC29543 zone)

SWISSPROT: IXTPA_ACIBT

ID   IXTPA_ACIBT             Reviewed;         207 AA.
AC   A3M1X9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   16-JAN-2019, entry version 69.
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=A1S_0468;
OS   Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 /
OS   NCDC KC755 / 5377).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=400667;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX   PubMed=17344419; DOI=10.1101/gad.1510307;
RA   Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA   Gerstein M., Snyder M.;
RT   "New insights into Acinetobacter baumannii pathogenesis revealed by
RT   high-density pyrosequencing and transposon mutagenesis.";
RL   Genes Dev. 21:601-614(2007).
CC   -!- FUNCTION: Pyrophosphatase that catalyzes the hydrolysis of
CC       nucleoside triphosphates to their monophosphate derivatives, with
CC       a high preference for the non-canonical purine nucleotides XTP
CC       (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and
CC       ITP. Seems to function as a house-cleaning enzyme that removes
CC       non-canonical purine nucleotides from the nucleotide pool, thus
CC       preventing their incorporation into DNA/RNA and avoiding
CC       chromosomal lesions. {ECO:0000255|HAMAP-Rule:MF_01405}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + XTP = diphosphate + H(+) + XMP;
CC         Xref=Rhea:RHEA:28610, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:61314;
CC         EC=3.6.1.66; Evidence={ECO:0000255|HAMAP-Rule:MF_01405};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dITP + H2O = dIMP + diphosphate + H(+);
CC         Xref=Rhea:RHEA:28342, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:61194, ChEBI:CHEBI:61382;
CC         EC=3.6.1.66; Evidence={ECO:0000255|HAMAP-Rule:MF_01405};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + ITP = diphosphate + H(+) + IMP;
CC         Xref=Rhea:RHEA:29399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58053, ChEBI:CHEBI:61402;
CC         EC=3.6.1.66; 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-
CC       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}.
DR   EMBL; CP000521; ABO10923.2; -; Genomic_DNA.
DR   SMR; A3M1X9; -.
DR   PRIDE; A3M1X9; -.
DR   EnsemblBacteria; ABO10923; ABO10923; A1S_0468.
DR   KEGG; acb:A1S_0468; -.
DR   HOGENOM; HOG000293319; -.
DR   KO; K02428; -.
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; IEA:UniProtKB-UniRule.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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;
DR   PRODOM; A3M1X9.
DR   SWISS-2DPAGE; A3M1X9.
KW   Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW   Nucleotide-binding.
FT   CHAIN         1    207       dITP/XTP pyrophosphatase.
FT                                /FTId=PRO_1000145479.
FT   REGION       16     21       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01405}.
FT   REGION      166    169       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01405}.
FT   REGION      194    195       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01405}.
FT   ACT_SITE     79     79       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01405}.
FT   METAL        79     79       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01405}.
FT   BINDING      80     80       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01405}.
FT   BINDING     189    189       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01405}.
SQ   SEQUENCE   207 AA;  22673 MW;  47FF6F388B73EE29 CRC64;
     MSTPHWFDQG SLVLASNNKG KVAEFEKLFE QLKLPVEIIP QGRLNIPDAI EDGLSFIENA
     IIKARHASKI SGKPAMADDS GICVPVLGGA PGIYSARYAG EHGDDAANNA KLLNDLLPFR
     KNGEVIEGMF VCVLALVTHA EDPLPQIFQG IWHGEILEAP RGENGFGYDP LFWLPELQVS
     SAELSKEEKN KISHRGQAMQ LFRESLV
//

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