ID B6J602_COXB1 Unreviewed; 200 AA.
AC B6J602;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 01-MAY-2013, entry version 30.
DE RecName: Full=Non-canonical purine NTP pyrophosphatase;
DE EC=3.6.1.19;
DE AltName: Full=Non-standard purine NTP pyrophosphatase;
DE AltName: Full=Nucleoside-triphosphate diphosphatase;
DE AltName: Full=Nucleoside-triphosphate pyrophosphatase;
GN OrderedLocusNames=CbuK_1988;
OS Coxiella burnetii (strain CbuK_Q154) (Coxiella burnetii (strain
OS Q154)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Coxiellaceae; Coxiella.
OX NCBI_TaxID=434924;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CbuK_Q154;
RX PubMed=19047403; DOI=10.1128/IAI.01141-08;
RA Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D.,
RA Williams K.P., Sobral B.W., Kupko J.J.III., Porcella S.F.,
RA Samuel J.E., Heinzen R.A.;
RT "Comparative genomics reveal extensive transposon-mediated genomic
RT plasticity and diversity among potential effector proteins within the
RT genus Coxiella.";
RL Infect. Immun. 77:642-656(2009).
CC -!- FUNCTION: Pyrophosphatase that hydrolyzes non-canonical purine
CC nucleotides such as XTP and ITP/dITP to their respective
CC monophosphate derivatives. Might exclude non-canonical purines
CC from DNA precursor pool, thus preventing their incorporation into
CC DNA and avoiding chromosomal lesions (By similarity).
CC -!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a
CC nucleotide + diphosphate.
CC -!- COFACTOR: Binds 1 divalent metal cation ion per subunit; can use
CC either magnesium or manganese (By similarity).
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SIMILARITY: Belongs to the HAM1 NTPase family.
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DR EMBL; CP001020; ACJ21093.1; -; Genomic_DNA.
DR RefSeq; YP_002306238.1; NC_011528.1.
DR ProteinModelPortal; B6J602; -.
DR SMR; B6J602; 1-195.
DR STRING; 434924.CbuK_1988; -.
DR EnsemblBacteria; ACJ21093; ACJ21093; CbuK_1988.
DR GeneID; 7016501; -.
DR KEGG; cbc:CbuK_1988; -.
DR PATRIC; 17919423; VBICoxBur77120_1988.
DR eggNOG; COG0127; -.
DR HOGENOM; HOG000293319; -.
DR KO; K02428; -.
DR ProtClustDB; PRK00120; -.
DR BioCyc; CBUR434924:GHWU-1983-MONOMER; -.
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:HAMAP.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0009143; P:nucleoside triphosphate catabolic process; IEA:InterPro.
DR GO; GO:0006163; P:purine nucleotide metabolic process; IEA:HAMAP.
DR HAMAP; MF_01405; Non_canon_purine_NTPase; 1; -.
DR InterPro; IPR002637; Ham1p-like.
DR InterPro; IPR020922; Nucleoside-triphosphatase.
DR PANTHER; PTHR11067; PTHR11067; 1.
DR Pfam; PF01725; Ham1p_like; 1.
DR TIGRFAMs; TIGR00042; TIGR00042; 1.
PE 3: Inferred from homology;
KW Complete proteome; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Nucleotide metabolism; Nucleotide-binding.
FT REGION 8 13 Substrate binding (By similarity).
FT REGION 69 70 Substrate binding (By similarity).
FT METAL 40 40 Magnesium or manganese (By similarity).
FT METAL 69 69 Magnesium or manganese (By similarity).
FT BINDING 157 157 Substrate (By similarity).
FT BINDING 177 177 Substrate (By similarity).
FT BINDING 183 183 Substrate (By similarity).
SQ SEQUENCE 200 AA; 21777 MW; A35DF16EE7025113 CRC64;
MLEIVLASQN SSKLAEMQEL LRDLEIKFIP QTEFSVPDIE ETGSTFVENA IIKARHAAKQ
TGLPALADDS GLTIAALNSA PGVFSSRYAG KNATDAERIQ KVLEALEAAD DSDRSASFHC
VIALMENEND PAPLICHGVW EGEIAREPRG KNGFGYDPIF YVPSHQRTAA ELDPQEKNAI
SHRGQALEQL STVLTEAFLV
//
