ID   RPPH_PSEPK              Reviewed;         159 AA.
AC   Q88CN4;
DT   06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=RNA pyrophosphohydrolase {ECO:0000255|HAMAP-Rule:MF_00298};
DE            EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_00298};
DE   AltName: Full=(Di)nucleoside polyphosphate hydrolase {ECO:0000255|HAMAP-Rule:MF_00298};
GN   Name=rppH {ECO:0000255|HAMAP-Rule:MF_00298};
GN   Synonyms=nudH {ECO:0000255|HAMAP-Rule:MF_00298}; OrderedLocusNames=PP_5146;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA   Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA   Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA   Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA   Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
CC   -!- FUNCTION: Accelerates the degradation of transcripts by removing
CC       pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a
CC       more labile monophosphorylated state that can stimulate subsequent
CC       ribonuclease cleavage. {ECO:0000255|HAMAP-Rule:MF_00298}.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00298};
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. RppH subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00298}.
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DR   EMBL; AE015451; AAN70711.1; -; Genomic_DNA.
DR   RefSeq; NP_747247.1; NC_002947.4.
DR   RefSeq; WP_003249017.1; NC_002947.4.
DR   AlphaFoldDB; Q88CN4; -.
DR   SMR; Q88CN4; -.
DR   STRING; 160488.PP_5146; -.
DR   EnsemblBacteria; AAN70711; AAN70711; PP_5146.
DR   GeneID; 58534079; -.
DR   GeneID; 61774619; -.
DR   GeneID; 66675116; -.
DR   KEGG; ppu:PP_5146; -.
DR   PATRIC; fig|160488.4.peg.5493; -.
DR   eggNOG; COG0494; Bacteria.
DR   HOGENOM; CLU_087195_3_1_6; -.
DR   OMA; PCVGIML; -.
DR   PhylomeDB; Q88CN4; -.
DR   BioCyc; PPUT160488:G1G01-5491-MON; -.
DR   Proteomes; UP000000556; Chromosome.
DR   GO; GO:0016462; F:pyrophosphatase activity; IEA:UniProt.
DR   CDD; cd03671; Ap4A_hydrolase_plant_like; 1.
DR   HAMAP; MF_00298; Nudix_RppH; 1.
DR   InterPro; IPR020476; Nudix_hydrolase.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR020084; NUDIX_hydrolase_CS.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   InterPro; IPR022927; RppH.
DR   Pfam; PF00293; NUDIX; 1.
DR   PRINTS; PR00502; NUDIXFAMILY.
DR   SUPFAM; SSF55811; SSF55811; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..159
FT                   /note="RNA pyrophosphohydrolase"
FT                   /id="PRO_0000057018"
FT   DOMAIN          6..149
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00298"
FT   MOTIF           38..59
FT                   /note="Nudix box"
SQ   SEQUENCE   159 AA;  18838 MW;  0E87C790942C2EDE CRC64;
     MIDPDGFRPN VGIILTNDAG QVLWARRINQ DAWQFPQGGI NPDETPEDAL YRELNEEVGL
     ERDDVEILAC TRGWLRYRLP QRLVRTHSQP LCIGQKQKWF LLRLVSNEQR VRMDLTGKPE
     FDGWRWVSYW YPLGQVVTFK REVYRRALKE LAPRLLTRD