ID A0A015TZ89_BACFG Unreviewed; 193 AA. AC A0A015TZ89; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 10-APR-2019, entry version 19. 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 CC dTTP and UTP. May have a dual role in cell division arrest and in CC preventing the incorporation of modified nucleotides into cellular CC nucleic acids. {ECO:0000256|HAMAP-Rule:MF_00528}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + UTP = diphosphate + H(+) + UMP; CC Xref=Rhea:RHEA:29395, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:57865; CC EC=3.6.1.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00528}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dTTP + H2O = diphosphate + dTMP + H(+); CC Xref=Rhea:RHEA:28534, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:63528; CC EC=3.6.1.9; 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 ECO:0000256|SAAS:SAAS01154128}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00528, CC ECO:0000256|SAAS:SAAS00965376}. 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 CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00528}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EXY89664.1}. 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; JGDB01000232; EXY89664.1; -; Genomic_DNA. DR RefSeq; WP_008769613.1; NZ_JGDB01000232.1. DR SMR; A0A015TZ89; -. DR EnsemblBacteria; EXY89664; EXY89664; M125_3647. 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:0047429; F:nucleoside-triphosphate diphosphatase activity; IEA:InterPro. 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. 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 Complete proteome {ECO:0000313|Proteomes:UP000020773}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00528, KW ECO:0000256|SAAS:SAAS00965379}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00528, KW ECO:0000256|SAAS:SAAS01154120}; KW Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_00528, KW ECO:0000256|SAAS:SAAS01154126}. FT ACT_SITE 77 77 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_00528}. FT SITE 18 18 Important for substrate specificity. FT {ECO:0000256|HAMAP-Rule:MF_00528}. FT SITE 78 78 Important for substrate specificity. FT {ECO:0000256|HAMAP-Rule:MF_00528}. FT SITE 160 160 Important for substrate specificity. FT {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 //