ID A3NC96_BURP6 Unreviewed; 210 AA.
AC A3NC96;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 01-MAY-2013, entry version 41.
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 Name=yggV; OrderedLocusNames=BURPS668_2952;
OS Burkholderia pseudomallei (strain 668).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=320373;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=668;
RA DeShazer D., Woods D.E., Nierman W.C.;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000570; ABN84617.1; -; Genomic_DNA.
DR RefSeq; YP_001059967.1; NC_009074.1.
DR STRING; 320373.BURPS668_2952; -.
DR EnsemblBacteria; ABN84617; ABN84617; BURPS668_2952.
DR GeneID; 4884551; -.
DR KEGG; bpd:BURPS668_2952; -.
DR PATRIC; 19251623; VBIBurPse82117_2748.
DR eggNOG; COG0127; -.
DR HOGENOM; HOG000293319; -.
DR KO; K02428; -.
DR OMA; DGTLVWP; -.
DR ProtClustDB; PRK00120; -.
DR BioCyc; BPSE320373:GJ9C-2945-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 19 24 Substrate binding (By similarity).
FT REGION 80 81 Substrate binding (By similarity).
FT METAL 51 51 Magnesium or manganese (By similarity).
FT METAL 80 80 Magnesium or manganese (By similarity).
FT BINDING 169 169 Substrate (By similarity).
FT BINDING 189 189 Substrate (By similarity).
FT BINDING 195 195 Substrate (By similarity).
SQ SEQUENCE 210 AA; 22179 MW; 8E696008CC5964DF CRC64;
MTMSHASPDA ARSRIVLASN NPGKLREFAA LFSTAGIDVV PQGELGVSEA DEPHATFVEN
ALAKARHASR ATGLPAVADD SGLCVPALLG APGVYSARYA QRAGREKSDA ANNAYLVEQL
REVADRRAYY YCVLALVRHA DDPEPLIAEG RWAGEILDAP RGAHGFGYDP HFFVPALGAT
AAELDPAAKN AASHRALALK ALVARLGEIR
//
