ID   A0A015TZ89_BACFG        Unreviewed;       193 AA.
AC   A0A015TZ89;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   02-JUN-2021, entry version 24.
DE   RecName: Full=dTTP/UTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_00528};
DE            Short=dTTPase/UTPase {ECO:0000256|HAMAP-Rule:MF_00528};
DE            EC=3.6.1.9 {ECO:0000256|HAMAP-Rule:MF_00528};
DE   AltName: Full=Nucleoside triphosphate pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_00528};
DE   AltName: Full=Nucleotide pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_00528};
DE            Short=Nucleotide PPase {ECO:0000256|HAMAP-Rule:MF_00528};
GN   Name=maf {ECO:0000313|EMBL:EXY89664.1};
GN   ORFNames=M125_3647 {ECO:0000313|EMBL:EXY89664.1};
OS   Bacteroides fragilis str. 3998T(B)3.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1339316 {ECO:0000313|EMBL:EXY89664.1, ECO:0000313|Proteomes:UP000020773};
RN   [1] {ECO:0000313|EMBL:EXY89664.1, ECO:0000313|Proteomes:UP000020773}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3998T(B)3 {ECO:0000313|Proteomes:UP000020773};
RA   Sears C., Carroll K., Sack B.R., Qadri F., Myers L.L., Chung G.-T.,
RA   Escheverria P., Fraser C.M., Sadzewicz L., Shefchek K.A., Tallon L.,
RA   Das S.P., Daugherty S., Mongodin E.F.;
RL   Submitted (FEB-2014) 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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00528};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00528};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00528}.
CC   -!- SIMILARITY: Belongs to the Maf family. YhdE subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00528}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00528}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EXY89664.1}.
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DR   EMBL; JGDB01000232; EXY89664.1; -; Genomic_DNA.
DR   RefSeq; WP_008769613.1; NZ_JGDB01000232.1.
DR   SMR; A0A015TZ89; -.
DR   GeneID; 60367438; -.
DR   GeneID; 61597444; -.
DR   PATRIC; fig|1339316.3.peg.3457; -.
DR   Proteomes; UP000020773; Unassembled WGS sequence.
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 {ECO:0000256|HAMAP-Rule:MF_00528};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00528};
KW   Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_00528}.
FT   ACT_SITE        77
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00528"
FT   SITE            18
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00528"
FT   SITE            78
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00528"
FT   SITE            160
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00528"
SQ   SEQUENCE   193 AA;  21681 MW;  E3CA27D3C264572F CRC64;
     MLANLDRYKI VLASNSPRRK ELMTGLGVDY VVKTLPDVDE SYPDTLQGEE IPLFIAREKA
     AAYQSMIGPE ELLITADTIV WHEGKALGKP VGRQDAIEML RSLSGKSHQV ITGVCLTTRE
     WQKCFAAVTD VRFAILDEDE IAYYVDHYQP MDKAGSYGVQ EWIGFVGVES ISGSYFNVMG
     LPIQKLYREL KQL
//