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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   05-JUL-2017, entry version 48.
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=Micau_1161 {ECO:0000313|EMBL:ADL44723.1};
OS   Micromonospora aurantiaca (strain ATCC 27029 / DSM 43813 / BCRC 12538
OS   / CBS 129.76 / JCM 10878 / NBRC 16125 / NRRL B-16091 / INA 9442).
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   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 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; CP002162; ADL44723.1; -; Genomic_DNA.
DR   RefSeq; WP_013284362.1; NC_014391.1.
DR   STRING; 644283.Micau_1161; -.
DR   EnsemblBacteria; ADL44723; ADL44723; Micau_1161.
DR   GeneID; 32161800; -.
DR   KEGG; mau:Micau_1161; -.
DR   eggNOG; ENOG4108V82; Bacteria.
DR   eggNOG; COG0127; LUCA.
DR   HOGENOM; HOG000293319; -.
DR   KO; K02428; -.
DR   OMA; YDPIFQP; -.
DR   OrthoDB; POG091H02BP; -.
DR   Proteomes; UP000001908; 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:UP000001908};
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:UP000001908}.
FT   REGION        8     13       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01405}.
FT   REGION      157    160       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01405}.
FT   REGION      185    186       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01405}.
FT   ACT_SITE     74     74       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01405}.
FT   METAL        74     74       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01405}.
FT   BINDING      75     75       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01405}.
FT   BINDING     180    180       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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