NTPPA_THET8
ID NTPPA_THET8 Reviewed; 187 AA.
AC Q5SJ26;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 88.
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=TTHA1188;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP008226; BAD71011.1; -; Genomic_DNA.
DR RefSeq; WP_011228501.1; NC_006461.1.
DR RefSeq; YP_144454.1; NC_006461.1.
DR AlphaFoldDB; Q5SJ26; -.
DR SMR; Q5SJ26; -.
DR STRING; 300852.55772570; -.
DR EnsemblBacteria; BAD71011; BAD71011; BAD71011.
DR GeneID; 3169011; -.
DR KEGG; ttj:TTHA1188; -.
DR PATRIC; fig|300852.9.peg.1169; -.
DR eggNOG; COG0424; Bacteria.
DR HOGENOM; CLU_040416_2_1_0; -.
DR OMA; RIDGDFY; -.
DR PhylomeDB; Q5SJ26; -.
DR Proteomes; UP000000532; 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..187
FT /note="dTTP/UTP pyrophosphatase"
FT /id="PRO_0000267454"
FT ACT_SITE 68
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT SITE 16
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT SITE 69
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT SITE 151
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
SQ SEQUENCE 187 AA; 20380 MW; 0BE0D134F3DCFD82 CRC64;
MGSGKPPLIL ASGSPRRKAL LEALGYPIRV AVPGVEEEGL PLPPKALAQA LARRKGEAVQ
GEWVLAADTV VDLDGEVLGK PKDPEENRLF LRRLSGRLHL VHTAFYLRTP KEVVEEVHTA
RVFFRPLSEE EIAWYVGSGE GLDKAGGYGA QGLGMALLER VEGDFYTVVG LPVSRVFALL
WARGFRP