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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   26-NOV-2014, entry version 27.
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=Micau_1161 {ECO:0000313|EMBL:ADL44723.1};
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 {ECO:0000313|EMBL:ADL44723.1, ECO:0000313|Proteomes:UP000001908};
RN   [1] {ECO:0000313|EMBL:ADL44723.1, ECO:0000313|Proteomes:UP000001908}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27029 / DSM 43813 / JCM 10878 / NBRC 16125 / INA 9442
RC   {ECO:0000313|Proteomes:UP000001908};
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. {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}.
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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; EAIIATH; -.
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   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:UP000001908};
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:UP000001908}.
FT   REGION        8     13       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01405}.
FT   REGION       74     75       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01405}.
FT   METAL        74     74       Magnesium or manganese.
FT                                {ECO:0000256|HAMAP-Rule:MF_01405}.
FT   BINDING     160    160       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01405}.
FT   BINDING     180    180       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01405}.
FT   BINDING     186    186       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01405}.
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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