ID   Q1QSA7_CHRSD            Unreviewed;       201 AA.
AC   Q1QSA7;
DT   16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2006, sequence version 1.
DT   07-SEP-2016, entry version 71.
DE   RecName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405, ECO:0000256|SAAS:SAAS00020486};
DE            EC=3.6.1.19 {ECO:0000256|HAMAP-Rule:MF_01405, ECO:0000256|SAAS:SAAS00020468};
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};
GN   OrderedLocusNames=Csal_3307 {ECO:0000313|EMBL:ABE60651.1};
OS   Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB
OS   13768).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Chromohalobacter.
OX   NCBI_TaxID=290398 {ECO:0000313|EMBL:ABE60651.1, ECO:0000313|Proteomes:UP000000239};
RN   [1] {ECO:0000313|Proteomes:UP000000239}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3043 / ATCC BAA-138 / NCIMB 13768
RC   {ECO:0000313|Proteomes:UP000000239};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Saunders E., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Csonka L.N.,
RA   O'Conner K., Vreeland R.H., Oren A., Vargas C., Nieto J., Arahal D.R.,
RA   Goodner B., Wheeler C., Hall P., Ewing A., Benson L., McBeath D.,
RA   Canovas D., Richardson P.;
RT   "Complete sequence of Chromohalobacter salexigens DSM 3043.";
RL   Submitted (MAR-2006) 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:SAAS00020483}.
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:SAAS00020467}.
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; CP000285; ABE60651.1; -; Genomic_DNA.
DR   RefSeq; WP_011508597.1; NC_007963.1.
DR   ProteinModelPortal; Q1QSA7; -.
DR   SMR; Q1QSA7; 5-198.
DR   STRING; 290398.Csal_3307; -.
DR   EnsemblBacteria; ABE60651; ABE60651; Csal_3307.
DR   KEGG; csa:Csal_3307; -.
DR   PATRIC; 21450494; VBIChrSal113723_3324.
DR   eggNOG; ENOG4108V82; Bacteria.
DR   eggNOG; COG0127; LUCA.
DR   HOGENOM; HOG000293319; -.
DR   KO; K02428; -.
DR   OMA; CEGLWHG; -.
DR   OrthoDB; POG091H02BP; -.
DR   Proteomes; UP000000239; 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: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   Complete proteome {ECO:0000313|Proteomes:UP000000239};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|RuleBase:RU003781, ECO:0000256|SAAS:SAAS00425982};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|SAAS:SAAS00425988};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|SAAS:SAAS00426004};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|SAAS:SAAS00425941};
KW   Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|SAAS:SAAS00425996};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|SAAS:SAAS00425966};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000239}.
FT   REGION       11     16       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01405}.
FT   REGION       72     73       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01405}.
FT   METAL        43     43       Magnesium or manganese.
FT                                {ECO:0000256|HAMAP-Rule:MF_01405}.
FT   METAL        72     72       Magnesium or manganese.
FT                                {ECO:0000256|HAMAP-Rule:MF_01405}.
FT   BINDING     160    160       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01405}.
FT   BINDING     180    180       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01405}.
FT   BINDING     186    186       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01405}.
SQ   SEQUENCE   201 AA;  21804 MW;  E9FC27509A7810D0 CRC64;
     MADQDTLVLA SGNTGKLREF QSLLAPLGLE VRPQRDFAVT EVEETGLTFV ENALLKAREA
     SRVSGLPALA DDSGLEVDAL QGAPGIRSAR FAGEPSDDAA NNRKLLEALK DVPEGQRGAR
     FWCVLVYLRH AEDPVPRIVQ CAWEGEVLAY PRGEGGFGYD SLFWVPERAM TAAELSAEDK
     NRLSHRGRAM QALLAQLSAP S
//