ID D2AT50_STRRD Unreviewed; 212 AA.
AC D2AT50;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 01-MAY-2013, entry version 28.
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=Sros_1735;
OS Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 /
OS NI 9100).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Streptosporangineae; Streptosporangiaceae; Streptosporangium.
OX NCBI_TaxID=479432;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100;
RX DOI=10.4056/sigs.631049;
RA Nolan M., Sikorski J., Jando M., Lucas S., Lapidus A.,
RA Glavina Del Rio T., Chen F., Tice H., Pitluck S., Cheng J.F.,
RA Chertkov O., Sims D., Meincke L., Brettin T., Han C., Detter J.C.,
RA Bruce D., Goodwin L., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Ivanova N., Mavromatis K., Mikhailova N., Chen A., Palaniappan K.,
RA Chain P., Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Streptosporangium roseum type strain (NI
RT 9100T).";
RL Stand. Genomic Sci. 2:29-37(2010).
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; CP001814; ACZ84726.1; -; Genomic_DNA.
DR RefSeq; YP_003337469.1; NC_013595.1.
DR EnsemblBacteria; ACZ84726; ACZ84726; Sros_1735.
DR GeneID; 8665012; -.
DR KEGG; sro:Sros_1735; -.
DR PATRIC; 32465413; VBIStrRos112010_1707.
DR HOGENOM; HOG000293319; -.
DR KO; K02428; -.
DR OMA; GEAHNDA; -.
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 20 25 Substrate binding (By similarity).
FT REGION 84 85 Substrate binding (By similarity).
FT METAL 84 84 Magnesium or manganese (By similarity).
FT BINDING 170 170 Substrate (By similarity).
FT BINDING 190 190 Substrate (By similarity).
FT BINDING 196 196 Substrate (By similarity).
SQ SEQUENCE 212 AA; 22172 MW; 6897E95AAD901023 CRC64;
MSAEPTGRPG VPADRVVLAT RNMGKIVELR RILADASVPV EIVGLEEFPE IGDVAETGLT
FAANALLKAH AVAQASGLPA IADDSGLCVD ALNGMPGIFS ARWSGRHGDD RANLELLLAQ
VSDVPREHRG AHFACAAALA LPSGQERVAE GSLHGLIIDA PRGTNGFGYD PIFLPDGESR
TTAELSAQEK DAISHRGRAF RALAPILAEV IS
//
