ID   RPPH_RICPR              Reviewed;         161 AA.
AC   Q9ZDT9;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=RNA pyrophosphohydrolase;
DE            EC=3.6.1.-;
DE   AltName: Full=(Di)nucleoside pentaphosphate pyrophosphatase;
DE   AltName: Full=(Di)nucleoside polyphosphate hydrolase;
DE   AltName: Full=Ap5A pyrophosphatase;
DE   AltName: Full=Protein InvA;
GN   Name=rppH; Synonyms=invA, nudH; OrderedLocusNames=RP236;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
RN   [2]
RP   CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
RC   STRAIN=Madrid E;
RX   PubMed=12096117; DOI=10.1074/mcp.m100030-mcp200;
RA   Gaywee J., Xu W., Radulovic S., Bessman M.J., Azad A.F.;
RT   "The Rickettsia prowazekii invasion gene homolog (invA) encodes a Nudix
RT   hydrolase active on adenosine (5')-pentaphospho-(5')-adenosine.";
RL   Mol. Cell. Proteomics 1:179-185(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 (By similarity). Preferentially hydrolyzes
CC       diadenosine penta-phosphate with ATP as one of the reaction products.
CC       Also able to hydrolyze diadenosine hexa-phosphate and diguanosine
CC       penta-phosphate. Has little or no activity on diadenosine tetra- and
CC       tri-phosphate, on diguanosine tetra- and tri-phosphate, on GDP-mannose,
CC       ADP-ribose, NADH and NAD(+). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:12096117};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:12096117};
CC       Note=Manganese cannot be used. {ECO:0000269|PubMed:12096117};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.5.;
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12096117}.
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. RppH subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AJ235271; CAA14698.1; -; Genomic_DNA.
DR   PIR; H71677; H71677.
DR   RefSeq; NP_220621.1; NC_000963.1.
DR   RefSeq; WP_004598539.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZDT9; -.
DR   SMR; Q9ZDT9; -.
DR   STRING; 272947.RP236; -.
DR   EnsemblBacteria; CAA14698; CAA14698; CAA14698.
DR   GeneID; 57569364; -.
DR   KEGG; rpr:RP236; -.
DR   PATRIC; fig|272947.5.peg.243; -.
DR   eggNOG; COG0494; Bacteria.
DR   HOGENOM; CLU_087195_3_0_5; -.
DR   OMA; PCVGIML; -.
DR   Proteomes; UP000002480; 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; 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   SUPFAM; SSF55811; SSF55811; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Magnesium; Reference proteome; Zinc.
FT   CHAIN           1..161
FT                   /note="RNA pyrophosphohydrolase"
FT                   /id="PRO_0000057025"
FT   DOMAIN          12..154
FT                   /note="Nudix hydrolase"
FT   MOTIF           46..67
FT                   /note="Nudix box"
SQ   SEQUENCE   161 AA;  18754 MW;  A1DFB99D9952A115 CRC64;
     MRNSSNKYLD LPYRPGVGMM ILNADNQIFV GKRIDTKISS WQMPQGGIVP GETPSIAAMR
     EMLEEIGSNK GYIIAESKCW YSYDVPSFLI PKLWNGNFRG QKQRWFLIRF TGNNKDINIH
     TSNPEFDQWR WTSLDELLSI IIPFKRKLYQ AVVKEFESLI Q