NTPPA_CAUVC
ID NTPPA_CAUVC Reviewed; 193 AA.
AC Q9A5V5;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=CC_2342;
OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
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; AE005673; AAK24313.1; -; Genomic_DNA.
DR PIR; E87539; E87539.
DR RefSeq; NP_421145.1; NC_002696.2.
DR AlphaFoldDB; Q9A5V5; -.
DR SMR; Q9A5V5; -.
DR STRING; 190650.CC_2342; -.
DR EnsemblBacteria; AAK24313; AAK24313; CC_2342.
DR KEGG; ccr:CC_2342; -.
DR PATRIC; fig|190650.5.peg.2363; -.
DR eggNOG; COG0424; Bacteria.
DR HOGENOM; CLU_040416_2_0_5; -.
DR OMA; RIDGDFY; -.
DR BioCyc; CAULO:CC2342-MON; -.
DR Proteomes; UP000001816; 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; Reference proteome.
FT CHAIN 1..193
FT /note="dTTP/UTP pyrophosphatase"
FT /id="PRO_0000123006"
FT ACT_SITE 73
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT SITE 15
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT SITE 74
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT SITE 157
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
SQ SEQUENCE 193 AA; 20423 MW; C050A84713FFED2B CRC64;
MAAGPALVLA SASPRRLDLL AQVGVTPDRV DPADIDETPL RDETPRRHAL RLALEKARVV
AARAPGDFVL AADTVVAVGR RILPKAETEA DVLYCLKLLS GRNHKVLTGV ALIAPDGRAA
TRLVETKVGF KRLSDAERDG YVASGQWRGK AGGYGVQGLA GGFITDLQGS YPSVVGLPLY
ETLNLLSGLG YRP
