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NTPPA_SHESR
ID   NTPPA_SHESR             Reviewed;         194 AA.
AC   Q0HZH0;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=Shewmr7_0482;
OS   Shewanella sp. (strain MR-7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=60481;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-7;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA   Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Shewanella sp. MR-7.";
RL   Submitted (AUG-2006) 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}.
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DR   EMBL; CP000444; ABI41485.1; -; Genomic_DNA.
DR   RefSeq; WP_011625003.1; NC_008322.1.
DR   AlphaFoldDB; Q0HZH0; -.
DR   SMR; Q0HZH0; -.
DR   EnsemblBacteria; ABI41485; ABI41485; Shewmr7_0482.
DR   KEGG; shm:Shewmr7_0482; -.
DR   HOGENOM; CLU_040416_2_1_6; -.
DR   OMA; RIDGDFY; -.
DR   OrthoDB; 1469203at2; -.
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..194
FT                   /note="dTTP/UTP pyrophosphatase"
FT                   /id="PRO_0000267429"
FT   ACT_SITE        76
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            77
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT   SITE            159
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
SQ   SEQUENCE   194 AA;  20547 MW;  4BB13DD0BBB855B8 CRC64;
     MNLVLASTSP RRKELLTHIG LGRAEFSFSQ VAPDIDETPK AGELPRDYVQ RLAAEKALAG
     LALCSGMSQP AVLGSDTIVV LENEILGKPV DEADAKRVLR ALSGKAHTVM TAVALAKADQ
     TSVRLVETLV RFCVLSDADI DAYVASQEPM DKAGSYGIQG LGGCFVESIE GSYSCVVGLP
     LVETRELLSE AGIR
 
 
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