GenomeNet

Database: UniProt/TrEMBL
Entry: D2AT50_STRRD
LinkDB: D2AT50_STRRD
Original site: D2AT50_STRRD 
ID   D2AT50_STRRD            Unreviewed;       212 AA.
AC   D2AT50;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   26-NOV-2014, entry version 37.
DE   RecName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405, ECO:0000256|SAAS:SAAS00101763};
DE            EC=3.6.1.19 {ECO:0000256|HAMAP-Rule:MF_01405, ECO:0000256|SAAS:SAAS00101728};
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=Sros_1735 {ECO:0000313|EMBL:ACZ84726.1};
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 {ECO:0000313|EMBL:ACZ84726.1, ECO:0000313|Proteomes:UP000002029};
RN   [1] {ECO:0000313|Proteomes:UP000002029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100
RC   {ECO:0000313|Proteomes:UP000002029};
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).
RN   [2] {ECO:0000313|EMBL:ACZ84726.1, ECO:0000313|Proteomes:UP000002029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100
RC   {ECO:0000313|Proteomes:UP000002029};
RX   PubMed=21304675;
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., Goeker 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   9100).";
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. {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       Note=Binds 1 divalent metal cation ion per subunit; can use either
CC       magnesium or manganese. {ECO:0000256|HAMAP-Rule:MF_01405,
CC       ECO:0000256|SAAS:SAAS00101777};
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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001814; ACZ84726.1; -; Genomic_DNA.
DR   RefSeq; WP_012888471.1; NC_013595.1.
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; VIDEERG; -.
DR   OrthoDB; EOG6CZQQP; -.
DR   BioCyc; SROS479432:GI0V-1749-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   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:UP000002029};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|RuleBase:RU003781};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|SAAS:SAAS00101735};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|SAAS:SAAS00101759};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|SAAS:SAAS00101767};
KW   Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|SAAS:SAAS00101755};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|SAAS:SAAS00101739};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002029}.
FT   REGION       20     25       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01405}.
FT   REGION       84     85       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01405}.
FT   METAL        84     84       Magnesium or manganese.
FT                                {ECO:0000256|HAMAP-Rule:MF_01405}.
FT   BINDING     170    170       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01405}.
FT   BINDING     190    190       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01405}.
FT   BINDING     196    196       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01405}.
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
//
DBGET integrated database retrieval system