ID D9TD85_MICAI Unreviewed; 205 AA.
AC D9TD85;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 01-MAY-2013, entry version 19.
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: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 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
//
