ID   F8LBA9_9CHLA            Unreviewed;       200 AA.
AC   F8LBA9;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   19-FEB-2014, entry version 8.
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=hamA; ORFNames=WCH_BS10310;
OS   Waddlia chondrophila 2032/99.
OC   Bacteria; Chlamydiae; Chlamydiales; Waddliaceae; Waddlia.
OX   NCBI_TaxID=765953;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=2032/99;
RA   Collingro A., Tischler P., Weinmaier T., Penz T., Heinz E.,
RA   Brunham R.C., Read T.D., Bavoil P.M., Sachse K., Kahane S.,
RA   Friedman M.G., Rattei T., Myers G.S.A., Horn M.;
RT   "Unity in variety -- the pan-genome of the Chlamydiae.";
RL   Submitted (MAY-2011) 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.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FR872638; CCB90773.1; -; Genomic_DNA.
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:0009143; P:nucleoside triphosphate catabolic process; IEA:InterPro.
DR   GO; GO:0006163; P:purine nucleotide metabolic process; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_01405; Non_canon_purine_NTPase; 1.
DR   InterPro; IPR002637; Ham1p-like.
DR   InterPro; IPR020922; NTPase.
DR   PANTHER; PTHR11067; PTHR11067; 1.
DR   Pfam; PF01725; Ham1p_like; 1.
DR   TIGRFAMs; TIGR00042; TIGR00042; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Manganese; Metal-binding; Nucleotide metabolism;
KW   Nucleotide-binding.
FT   REGION        7     12       Substrate binding (By similarity).
FT   REGION       70     71       Substrate binding (By similarity).
FT   METAL        41     41       Magnesium or manganese (By similarity).
FT   METAL        70     70       Magnesium or manganese (By similarity).
FT   BINDING     156    156       Substrate (By similarity).
FT   BINDING     176    176       Substrate (By similarity).
FT   BINDING     182    182       Substrate (By similarity).
SQ   SEQUENCE   200 AA;  22620 MW;  30CDEA02925288CA CRC64;
     MELILATHNL HKIREFRQIL KEVKGLDLIS LRNFPDYQLP EETGKTFQEN ADLKALHAAK
     MLKAIVLADD SGLVVPALQG APGIYSARYA SSDATDKENR EKLMQEMEKF EDLDRSAYYE
     CCITIAGPEG ILKTAKATCE GLIGEQEKGR NGFGYDPIFI KHDYDKTFAE LEEQTKNRIS
     HRRKALDKIL AFLEAQIPSE
//