ID   F8LBA9_9CHLA            Unreviewed;       200 AA.
AC   F8LBA9;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   18-JAN-2017, entry version 23.
DE   RecName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405};
DE            EC=3.6.1.9 {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};
DE   AltName: Full=Nucleotide diphosphatase {ECO:0000256|HAMAP-Rule:MF_01405};
GN   Name=hamA {ECO:0000313|EMBL:CCB90773.1};
GN   ORFNames=WCH_BS10310 {ECO:0000313|EMBL:CCB90773.1};
OS   Waddlia chondrophila 2032/99.
OC   Bacteria; Chlamydiae; Chlamydiales; Waddliaceae; Waddlia.
OX   NCBI_TaxID=765953 {ECO:0000313|EMBL:CCB90773.1};
RN   [1] {ECO:0000313|EMBL:CCB90773.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=2032/99 {ECO:0000313|EMBL:CCB90773.1};
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. {ECO:0000256|HAMAP-
CC       Rule:MF_01405}.
CC   -!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a
CC       nucleotide + diphosphate. {ECO:0000256|HAMAP-Rule:MF_01405,
CC       ECO:0000256|SAAS:SAAS00101772}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01405};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01405};
CC       Note=Binds 1 divalent metal cation per subunit; can use either
CC       Mg(2+) or Mn(2+). {ECO:0000256|HAMAP-Rule:MF_01405};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|SAAS:SAAS00608136};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01405,
CC       ECO:0000256|SAAS:SAAS00101722}.
CC   -!- SIMILARITY: Belongs to the HAM1 NTPase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01405, ECO:0000256|RuleBase:RU003781,
CC       ECO:0000256|SAAS:SAAS00542593}.
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DR   EMBL; FR872638; CCB90773.1; -; Genomic_DNA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0035529; F:NADH pyrophosphatase activity; IEA:UniProtKB-EC.
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   CDD; cd00515; HAM1; 1.
DR   Gene3D; 3.90.950.10; -; 1.
DR   HAMAP; MF_01405; Non_canon_purine_NTPase; 1.
DR   InterPro; IPR002637; Ham1p-like.
DR   InterPro; IPR029001; ITPase-like_fam.
DR   InterPro; IPR020922; NTPase.
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;
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|RuleBase:RU003781, ECO:0000256|SAAS:SAAS00020484,
KW   ECO:0000313|EMBL:CCB90773.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|SAAS:SAAS00020482};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|SAAS:SAAS00020469};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|SAAS:SAAS00020489};
KW   Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|SAAS:SAAS00020487};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|SAAS:SAAS00020485}.
FT   REGION        7     12       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01405}.
FT   REGION       70     71       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01405}.
FT   METAL        41     41       Magnesium or manganese.
FT                                {ECO:0000256|HAMAP-Rule:MF_01405}.
FT   METAL        70     70       Magnesium or manganese.
FT                                {ECO:0000256|HAMAP-Rule:MF_01405}.
FT   BINDING     156    156       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01405}.
FT   BINDING     176    176       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01405}.
FT   BINDING     182    182       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01405}.
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
//