(data stored in ACNUC7421 zone)

SWISSPROT: NTPP_RHOPS

ID   NTPP_RHOPS              Reviewed;         202 AA.
AC   Q13E26;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 67.
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=RPD_0425;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Nucleoside triphosphate pyrophosphatase. May have a dual
CC       role in cell division arrest and in preventing the incorporation
CC       of modified nucleotides into cellular nucleic acids.
CC       {ECO:0000255|HAMAP-Rule:MF_00528}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside
CC         5'-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;
CC         EC=3.6.1.9; 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}.
DR   EMBL; CP000283; ABE37663.1; -; Genomic_DNA.
DR   RefSeq; WP_011500851.1; NC_007958.1.
DR   SMR; Q13E26; -.
DR   STRING; 316057.RPD_0425; -.
DR   EnsemblBacteria; ABE37663; ABE37663; RPD_0425.
DR   KEGG; rpd:RPD_0425; -.
DR   eggNOG; ENOG4108UHJ; Bacteria.
DR   eggNOG; COG0424; LUCA.
DR   HOGENOM; HOG000241744; -.
DR   KO; K06287; -.
DR   OMA; CAGSFKA; -.
DR   OrthoDB; 1469203at2; -.
DR   BioCyc; RPAL316057:RPD_RS02185-MONOMER; -.
DR   Proteomes; UP000001818; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0035529; F:NADH pyrophosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IEA:InterPro.
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.
PE   3: Inferred from homology;
DR   PRODOM; Q13E26.
DR   SWISS-2DPAGE; Q13E26.
KW   Complete proteome; Cytoplasm; Hydrolase; Nucleotide metabolism.
FT   CHAIN         1    202       Nucleoside triphosphate pyrophosphatase.
FT                                /FTId=PRO_0000267404.
FT   ACT_SITE     79     79       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00528}.
SQ   SEQUENCE   202 AA;  21604 MW;  A278B691B5F3AA49 CRC64;
     MTLWLGPQPL VLASQSRARQ ALLTNAGIPF EAIPAKLDER GIARVSGLSA PGDIAALLAQ
     EKAAFVSNHH PGRLVLGADQ TLALGAREFN KPADRNEAAK QLRELAGRRH ELHSAIAVVR
     NGITLFAEVV IARMTMRPLS DEEIAVYLDE VGDTATCSVG GYQVEGLGVH LFDGIHGDHS
     TILGLPLLPL LGFLRSQKLL TL
//

If you have problems or comments...

PBIL Back to PBIL home page