ID   NTPPA_GEOKA             Reviewed;         186 AA.
AC   Q5KWN2;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 84.
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   Name=maf; OrderedLocusNames=GK2619;
OS   Geobacillus kaustophilus (strain HTA426).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=235909;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTA426;
RX   PubMed=15576355; DOI=10.1093/nar/gkh970;
RA   Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA   Matsui S., Uchiyama I.;
RT   "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT   Geobacillus kaustophilus.";
RL   Nucleic Acids Res. 32:6292-6303(2004).
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; BA000043; BAD76904.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5KWN2; -.
DR   SMR; Q5KWN2; -.
DR   STRING; 235909.GK2619; -.
DR   EnsemblBacteria; BAD76904; BAD76904; GK2619.
DR   KEGG; gka:GK2619; -.
DR   eggNOG; COG0424; Bacteria.
DR   HOGENOM; CLU_040416_0_0_9; -.
DR   OMA; RIDGDFY; -.
DR   Proteomes; UP000001172; 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..186
FT                   /note="dTTP/UTP pyrophosphatase"
FT                   /id="PRO_0000267234"
FT   ACT_SITE        65
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT   SITE            8
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT   SITE            66
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT   SITE            149
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
SQ   SEQUENCE   186 AA;  20434 MW;  1132623A88866A46 CRC64;
     MLASRSPRRR QILELAGWPF DVQESHADET IPPGTPPDEA VQLLARRKVE AVMSSFPDAY
     VLGADTIVVC DGRLLGKPRT EEEAFAMLRQ LSGRTHDVWT GVAIALPQGS ITSFAEKTAV
     TFWELDDEEI AAYIATGEPM DKAGAYGIQG RAALFVKRIE GDYLTVVGLP LSRTVRELRR
     LGWPPA