NTPP_CUTAK
ID NTPP_CUTAK Reviewed; 213 AA.
AC Q6A725;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Nucleoside triphosphate pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00528};
DE EC=3.6.1.9 {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=PPA1709;
OS Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS acnes).
OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC Cutibacterium.
OX NCBI_TaxID=267747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16379 / KPA171202;
RX PubMed=15286373; DOI=10.1126/science.1100330;
RA Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA Strittmatter A., Hujer S., Duerre P., Gottschalk G.;
RT "The complete genome sequence of Propionibacterium acnes, a commensal of
RT human skin.";
RL Science 305:671-673(2004).
CC -!- FUNCTION: Nucleoside triphosphate pyrophosphatase. May have a dual role
CC in cell division arrest and in preventing the incorporation of modified
CC nucleotides into cellular nucleic acids. {ECO:0000255|HAMAP-
CC Rule:MF_00528}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC phosphate + diphosphate + H(+); Xref=Rhea:RHEA:23996,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00528};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'-
CC deoxyribonucleoside 5'-phosphate + diphosphate + H(+);
CC Xref=Rhea:RHEA:44644, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:65317; 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. {ECO:0000255|HAMAP-
CC Rule:MF_00528}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAT83440.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE017283; AAT83440.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_014167039.1; NZ_CP025935.1.
DR AlphaFoldDB; Q6A725; -.
DR SMR; Q6A725; -.
DR STRING; 267747.PPA1709; -.
DR PRIDE; Q6A725; -.
DR EnsemblBacteria; AAT83440; AAT83440; PPA1709.
DR KEGG; pac:PPA1709; -.
DR eggNOG; COG0424; Bacteria.
DR HOGENOM; CLU_040416_1_2_11; -.
DR OMA; RIDGDFY; -.
DR Proteomes; UP000000603; 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: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..213
FT /note="Nucleoside triphosphate pyrophosphatase"
FT /id="PRO_0000267372"
FT ACT_SITE 77
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
SQ SEQUENCE 213 AA; 22969 MW; 11E9CF2B98951F7D CRC64;
MTTCFVLASK SPARLRMLRS AGIEPVVIAS GADESHLRGE DAVAMTARLS RLKAHSVIES
GALEEYPADR MIVVACDSVL NLDGRILGKP HTAERARQWW RRMRGHQGVL VSGHHVAVIV
NGQLREQTRI GQTVVTFADL TDAEIDAYVD SGEPAAVAGA FTIDGLGGAF ITRINGDPHN
VTGISLPLLR QMLMDLDVEW SSLWNGPKGG HLS