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Database: UniProt/TrEMBL
Entry: D9TD85_MICAI
LinkDB: D9TD85_MICAI
Original site: D9TD85_MICAI 
ID   D9TD85_MICAI            Unreviewed;       205 AA.
AC   D9TD85;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   19-FEB-2014, entry version 22.
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=Micau_1161;
OS   Micromonospora aurantiaca (strain ATCC 27029 / DSM 43813 / JCM 10878 /
OS   NBRC 16125 / INA 9442).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micromonosporineae; Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=644283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27029 / DSM 43813 / JCM 10878 / NBRC 16125 / INA 9442;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Hirsch A.M., Woyke T.;
RT   "Complete sequence of Micromonospora aurantiaca ATCC 27029.";
RL   Submitted (AUG-2010) 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; CP002162; ADL44723.1; -; Genomic_DNA.
DR   RefSeq; YP_003834299.1; NC_014391.1.
DR   EnsemblBacteria; ADL44723; ADL44723; Micau_1161.
DR   GeneID; 9599231; -.
DR   KEGG; mau:Micau_1161; -.
DR   PATRIC; 42388023; VBIMicAur74833_1180.
DR   HOGENOM; HOG000293319; -.
DR   KO; K02428; -.
DR   OMA; GEAHNDA; -.
DR   BioCyc; MAUR644283:GHOD-1176-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: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   Complete proteome; Hydrolase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide metabolism; Nucleotide-binding.
FT   REGION        8     13       Substrate binding (By similarity).
FT   REGION       74     75       Substrate binding (By similarity).
FT   METAL        74     74       Magnesium or manganese (By similarity).
FT   BINDING     160    160       Substrate (By similarity).
FT   BINDING     180    180       Substrate (By similarity).
FT   BINDING     186    186       Substrate (By similarity).
SQ   SEQUENCE   205 AA;  21912 MW;  7198EE5A56F539D9 CRC64;
     MNKVLLATRN RKKLVELQRI LDGALGAHRI ALLGLDDVEE YPELPETGLT FGENALIKAR
     EGCRRTGLPT IADDSGLAVD ALNGMPGVFS ARWSGGHGDD RANLQLVLDQ VADVPDEHRG
     AAFVCTVALV LPGGKEHLVD GRQSGRLLRA PRGDGGFGYD PIFLGDGQER TNAELTPEEK
     DAVSHRGKAL RELAKLVAKV LPPAA
//
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