ID   NTPPA_GLUOX             Reviewed;         218 AA.
AC   Q5FS71;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=dTTP/UTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00528};
DE            Short=dTTPase/UTPase {ECO:0000255|HAMAP-Rule:MF_00528};
DE            EC=3.6.1.9 {ECO:0000255|HAMAP-Rule:MF_00528};
DE   AltName: Full=Nucleoside triphosphate pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00528};
DE   AltName: Full=Nucleotide pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00528};
DE            Short=Nucleotide PPase {ECO:0000255|HAMAP-Rule:MF_00528};
GN   OrderedLocusNames=GOX1003;
OS   Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=290633;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=621H;
RX   PubMed=15665824; DOI=10.1038/nbt1062;
RA   Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA   Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT   "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT   oxydans.";
RL   Nat. Biotechnol. 23:195-200(2005).
CC   -!- FUNCTION: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP
CC       and UTP. May have a dual role in cell division arrest and in preventing
CC       the incorporation of modified nucleotides into cellular nucleic acids.
CC       {ECO:0000255|HAMAP-Rule:MF_00528}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dTTP + H2O = diphosphate + dTMP + H(+); Xref=Rhea:RHEA:28534,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:37568, ChEBI:CHEBI:63528; EC=3.6.1.9;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00528};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + UTP = diphosphate + H(+) + UMP; Xref=Rhea:RHEA:29395,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:46398, ChEBI:CHEBI:57865; EC=3.6.1.9;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00528};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00528};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00528}.
CC   -!- SIMILARITY: Belongs to the Maf family. YhdE subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00528}.
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DR   EMBL; CP000009; AAW60775.1; -; Genomic_DNA.
DR   RefSeq; WP_011252568.1; NZ_LT900338.1.
DR   AlphaFoldDB; Q5FS71; -.
DR   SMR; Q5FS71; -.
DR   STRING; 290633.GOX1003; -.
DR   EnsemblBacteria; AAW60775; AAW60775; GOX1003.
DR   KEGG; gox:GOX1003; -.
DR   eggNOG; COG0424; Bacteria.
DR   HOGENOM; CLU_040416_2_0_5; -.
DR   OMA; RIDGDFY; -.
DR   Proteomes; UP000006375; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0036218; F:dTTP diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0035529; F:NADH pyrophosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0036221; F:UTP diphosphatase activity; IEA:RHEA.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00555; Maf; 1.
DR   Gene3D; 3.90.950.10; -; 1.
DR   HAMAP; MF_00528; Maf; 1.
DR   InterPro; IPR029001; ITPase-like_fam.
DR   InterPro; IPR003697; Maf-like.
DR   PANTHER; PTHR43213; PTHR43213; 1.
DR   Pfam; PF02545; Maf; 1.
DR   PIRSF; PIRSF006305; Maf; 1.
DR   SUPFAM; SSF52972; SSF52972; 1.
DR   TIGRFAMs; TIGR00172; maf; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Nucleotide metabolism; Reference proteome.
FT   CHAIN           1..218
FT                   /note="dTTP/UTP pyrophosphatase"
FT                   /id="PRO_0000267314"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        87
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT   SITE            28
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT   SITE            88
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT   SITE            175
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
SQ   SEQUENCE   218 AA;  22919 MW;  3E15EB3640A3DD1E CRC64;
     MTASPSSAEG SSGLPDRPKL VLASASPRRL SLLEQIGIVP DAVVSADIDE EPRPGELPRP
     LAQRLARQKA EHVAAQRTDA ALVLGADTVV SVGRRVLPKA EDEKTARACL KLLSGRRHKV
     LTAVVLRPSA GWPQGTPCER LVETSVIFHR LTDAQIDALI AQGDWQGKAG GYAIQGAAAA
     HIRQIGGSYS AVVGLPLFET AQLLRGQPVG KPSGGWIA