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NTPPA_BACFR
ID   NTPPA_BACFR             Reviewed;         193 AA.
AC   Q64R56;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=BF3281;
OS   Bacteroides fragilis (strain YCH46).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=295405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCH46;
RX   PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA   Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA   Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT   "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT   regulating cell surface adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(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; AP006841; BAD50025.1; -; Genomic_DNA.
DR   RefSeq; WP_011203220.1; NC_006347.1.
DR   RefSeq; YP_100559.1; NC_006347.1.
DR   AlphaFoldDB; Q64R56; -.
DR   SMR; Q64R56; -.
DR   STRING; 295405.BF3281; -.
DR   EnsemblBacteria; BAD50025; BAD50025; BF3281.
DR   KEGG; bfr:BF3281; -.
DR   PATRIC; fig|295405.11.peg.3152; -.
DR   HOGENOM; CLU_040416_0_0_10; -.
DR   OMA; RIDGDFY; -.
DR   Proteomes; UP000002197; 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..193
FT                   /note="dTTP/UTP pyrophosphatase"
FT                   /id="PRO_0000267248"
FT   ACT_SITE        77
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT   SITE            18
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT   SITE            78
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT   SITE            160
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
SQ   SEQUENCE   193 AA;  21667 MW;  F3009DB3C278B9DD CRC64;
     MLANLDRYKI VLASNSPRRK ELMTGLGVDY VVKTLPDVDE SYPDTLQGEE IPLFIAREKA
     AAYQSMIGPE ELLITADTIV WHEGKALGKP VGRQDAIEML RSLSGKSHQV ITGVCVTTRE
     WQKCFAAVTD VRFAILDEDE IAYYVDHYQP MDKAGSYGVQ EWIGFVGVES ISGSYFNVMG
     LPIQKLYREL KQL
 
 
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