(data stored in SCRATCH zone)

SWISSPROT: A0A0H2ZKH4_PSEAB

ID   A0A0H2ZKH4_PSEAB        Unreviewed;       197 AA.
AC   A0A0H2ZKH4;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   07-JUN-2017, entry version 15.
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=PA14_05050 {ECO:0000313|EMBL:ABJ15353.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ15353.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ15353.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ15353.1,
RC   ECO:0000313|Proteomes:UP000000653};
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
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:0000256|HAMAP-Rule:MF_01405,
CC       ECO:0000256|SAAS:SAAS00805977}.
CC   -!- CATALYTIC ACTIVITY: ITP + H(2)O = IMP + diphosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_01405, ECO:0000256|SAAS:SAAS00805978}.
CC   -!- CATALYTIC ACTIVITY: XTP + H(2)O = XMP + diphosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_01405, ECO:0000256|SAAS:SAAS00805983}.
CC   -!- CATALYTIC ACTIVITY: dITP + H(2)O = dIMP + diphosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_01405, ECO:0000256|SAAS:SAAS00805979}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01405};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01405};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01405,
CC       ECO:0000256|SAAS:SAAS00730484}.
CC   -!- SIMILARITY: Belongs to the HAM1 NTPase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01405, ECO:0000256|RuleBase:RU003781,
CC       ECO:0000256|SAAS:SAAS00730348}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000438; ABJ15353.1; -; Genomic_DNA.
DR   RefSeq; WP_003084527.1; NC_008463.1.
DR   ProteinModelPortal; A0A0H2ZKH4; -.
DR   SMR; A0A0H2ZKH4; -.
DR   EnsemblBacteria; ABJ15353; ABJ15353; PA14_05050.
DR   KEGG; pau:PA14_05050; -.
DR   KO; K02428; -.
DR   OMA; YDPIFQP; -.
DR   Proteomes; UP000000653; Chromosome.
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-HAMAP.
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-HAMAP.
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; A0A0H2ZKH4.
DR   SWISS-2DPAGE; A0A0H2ZKH4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000653};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|RuleBase:RU003781, ECO:0000256|SAAS:SAAS00730407};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|SAAS:SAAS00730390};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|SAAS:SAAS00730432};
KW   Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|SAAS:SAAS00730340};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|SAAS:SAAS00730332}.
FT   REGION       11     16       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01405}.
FT   REGION      155    158       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01405}.
FT   REGION      183    184       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01405}.
FT   ACT_SITE     71     71       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01405}.
FT   METAL        42     42       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01405}.
FT   METAL        71     71       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01405}.
FT   BINDING      72     72       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01405}.
FT   BINDING     178    178       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01405}.
SQ   SEQUENCE   197 AA;  21242 MW;  778471EE9BD53531 CRC64;
     MIKLEQLVLA SHNAGKLKEL QAMLGASVKV RSIGEFSQVE PEETGLSFVE NAILKARNAA
     RLSGLPALAD DSGLAVDFLG GAPGIYSARY ADGRGDAANN AKLLEAMKDV PDAERGAQFV
     SVLALVRHAD DPLPILCEGI WEGRILREAR GAHGFGYDPL FWVPERDCSS AELAPEEKNR
     LSHRARAMAL LKQRLGL
//

If you have problems or comments...

PBIL Back to PBIL home page