NTPPA_THEM4
ID NTPPA_THEM4 Reviewed; 182 AA.
AC A6LJI7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=Tmel_0214;
OS Thermosipho melanesiensis (strain DSM 12029 / CIP 104789 / BI429).
OC Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae; Thermosipho.
OX NCBI_TaxID=391009;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12029 / CIP 104789 / BI429;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT "Complete sequence of Thermosipho melanesiensis BI429.";
RL Submitted (MAY-2007) 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; CP000716; ABR30088.1; -; Genomic_DNA.
DR RefSeq; WP_012056449.1; NC_009616.1.
DR AlphaFoldDB; A6LJI7; -.
DR SMR; A6LJI7; -.
DR STRING; 391009.Tmel_0214; -.
DR EnsemblBacteria; ABR30088; ABR30088; Tmel_0214.
DR KEGG; tme:Tmel_0214; -.
DR eggNOG; COG0424; Bacteria.
DR HOGENOM; CLU_040416_0_0_0; -.
DR OMA; RIDGDFY; -.
DR Proteomes; UP000001110; 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.
FT CHAIN 1..182
FT /note="dTTP/UTP pyrophosphatase"
FT /id="PRO_1000127798"
FT ACT_SITE 64
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT SITE 11
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT SITE 65
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT SITE 147
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
SQ SEQUENCE 182 AA; 20882 MW; D235016CC88C6AA8 CRC64;
MDIILATSSP RRINLLKMLN IKFKTVAPRI KENINETDPE KLVKKLSKLK ALSIKEKGII
ISADTIVYHN NKVLGKPKNL DNAFNMLKEL SSKWHTVYTG VTIIEKDDII TFCEKTMVKF
KKLSDELIRY YISTSKPLDK AGAYGIQELG AILVEKIEGD YYNVVGLPIS RIWDILWDRR
II
