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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   07-JUN-2017, entry version 58.
DE   RecName: Full=dITP/XTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405};
DE            EC=3.6.1.66 {ECO:0000256|HAMAP-Rule:MF_01405};
DE   AltName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405};
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};
DE            Short=NTPase {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; Streptosporangiales; Streptosporangiaceae;
OC   Streptosporangium.
OX   NCBI_TaxID=479432 {ECO:0000313|EMBL:ACZ84726.1, ECO:0000313|Proteomes:UP000002029};
RN   [1] {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; 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   9100).";
RL   Stand. Genomic Sci. 2:29-37(2010).
CC   -!- FUNCTION: Pyrophosphatase that catalyzes the hydrolysis of
CC       nucleoside triphosphates to their monophosphate derivatives, with
CC       a high preference for the non-canonical purine nucleotides XTP
CC       (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and
CC       ITP. Seems to function as a house-cleaning enzyme that removes
CC       non-canonical purine nucleotides from the nucleotide pool, thus
CC       preventing their incorporation into DNA/RNA and avoiding
CC       chromosomal lesions. {ECO:0000256|HAMAP-Rule:MF_01405,
CC       ECO:0000256|SAAS:SAAS00805977}.
CC   -!- CATALYTIC ACTIVITY: ITP + H(2)O = IMP + diphosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_01405, ECO:0000256|SAAS:SAAS00805978}.
CC   -!- CATALYTIC ACTIVITY: XTP + H(2)O = XMP + diphosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_01405, ECO:0000256|SAAS:SAAS00805983}.
CC   -!- CATALYTIC ACTIVITY: dITP + H(2)O = dIMP + diphosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_01405, ECO:0000256|SAAS:SAAS00805979}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01405};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01405};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01405,
CC       ECO:0000256|SAAS:SAAS00730484}.
CC   -!- SIMILARITY: Belongs to the HAM1 NTPase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01405, ECO:0000256|RuleBase:RU003781,
CC       ECO:0000256|SAAS:SAAS00730348}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01405}.
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DR   EMBL; CP001814; ACZ84726.1; -; Genomic_DNA.
DR   STRING; 479432.Sros_1735; -.
DR   EnsemblBacteria; ACZ84726; ACZ84726; Sros_1735.
DR   KEGG; sro:Sros_1735; -.
DR   eggNOG; ENOG4108V82; Bacteria.
DR   eggNOG; COG0127; LUCA.
DR   HOGENOM; HOG000293319; -.
DR   KO; K02428; -.
DR   OMA; YDPIFQP; -.
DR   OrthoDB; POG091H02BP; -.
DR   BioCyc; SROS479432:GI0V-1679-MONOMER; -.
DR   Proteomes; UP000002029; 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:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009146; P:purine nucleoside triphosphate catabolic 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; IPR020922; dITP/XTP_pyrophosphatase.
DR   InterPro; IPR002637; Ham1p-like.
DR   InterPro; IPR029001; ITPase-like_fam.
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, ECO:0000256|SAAS:SAAS00730407};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|SAAS:SAAS00730390};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|SAAS:SAAS00730432};
KW   Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|SAAS:SAAS00730340};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01405,
KW   ECO:0000256|SAAS:SAAS00730332};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002029}.
FT   REGION       20     25       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01405}.
FT   REGION      167    170       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01405}.
FT   REGION      195    196       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01405}.
FT   ACT_SITE     84     84       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01405}.
FT   METAL        84     84       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01405}.
FT   BINDING      85     85       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01405}.
FT   BINDING     190    190       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
//
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