ID   RPPH_GLUDA              Reviewed;         167 AA.
AC   A9H3A6; B5ZIW0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 88.
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};
GN   OrderedLocusNames=GDI3350, Gdia_3020;
OS   Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / CCUG 37298
OS   / CIP 103539 / LMG 7603 / PAl5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconacetobacter.
OX   NCBI_TaxID=272568;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49037 / DSM 5601 / CCUG 37298 / CIP 103539 / LMG 7603 / PAl5;
RX   PubMed=19775431; DOI=10.1186/1471-2164-10-450;
RA   Bertalan M., Albano R., de Padua V., Rouws L., Rojas C., Hemerly A.,
RA   Teixeira K., Schwab S., Araujo J., Oliveira A., Franca L., Magalhaes V.,
RA   Alqueres S., Cardoso A., Almeida W., Loureiro M.M., Nogueira E., Cidade D.,
RA   Oliveira D., Simao T., Macedo J., Valadao A., Dreschsel M., Freitas F.,
RA   Vidal M., Guedes H., Rodrigues E., Meneses C., Brioso P., Pozzer L.,
RA   Figueiredo D., Montano H., Junior J., de Souza Filho G.,
RA   Martin Quintana Flores V., Ferreira B., Branco A., Gonzalez P.,
RA   Guillobel H., Lemos M., Seibel L., Macedo J., Alves-Ferreira M.,
RA   Sachetto-Martins G., Coelho A., Santos E., Amaral G., Neves A.,
RA   Pacheco A.B., Carvalho D., Lery L., Bisch P., Rossle S.C., Urmenyi T.,
RA   Rael Pereira A., Silva R., Rondinelli E., von Kruger W., Martins O.,
RA   Baldani J.I., Ferreira P.C.;
RT   "Complete genome sequence of the sugarcane nitrogen-fixing endophyte
RT   Gluconacetobacter diazotrophicus Pal5.";
RL   BMC Genomics 10:450-450(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49037 / DSM 5601 / CCUG 37298 / CIP 103539 / LMG 7603 / PAl5;
RX   PubMed=21304715; DOI=10.4056/sigs.972221;
RA   Giongo A., Tyler H.L., Zipperer U.N., Triplett E.W.;
RT   "Two genome sequences of the same bacterial strain, Gluconacetobacter
RT   diazotrophicus PAl 5, suggest a new standard in genome sequence
RT   submission.";
RL   Stand. Genomic Sci. 2:309-317(2010).
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; AM889285; CAP57293.1; -; Genomic_DNA.
DR   EMBL; CP001189; ACI52750.1; -; Genomic_DNA.
DR   RefSeq; WP_012227855.1; NC_010125.1.
DR   AlphaFoldDB; A9H3A6; -.
DR   SMR; A9H3A6; -.
DR   STRING; 272568.GDI3350; -.
DR   EnsemblBacteria; ACI52750; ACI52750; Gdia_3020.
DR   EnsemblBacteria; CAP57293; CAP57293; GDI3350.
DR   KEGG; gdi:GDI3350; -.
DR   KEGG; gdj:Gdia_3020; -.
DR   eggNOG; COG1051; Bacteria.
DR   HOGENOM; CLU_087195_3_0_5; -.
DR   OMA; PLDCVIE; -.
DR   Proteomes; UP000000736; Chromosome.
DR   Proteomes; UP000001176; 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..167
FT                   /note="RNA pyrophosphohydrolase"
FT                   /id="PRO_1000078964"
FT   DOMAIN          8..158
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00298"
FT   MOTIF           49..70
FT                   /note="Nudix box"
FT   CONFLICT        6
FT                   /note="D -> T (in Ref. 2; ACI52750)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        21
FT                   /note="Q -> R (in Ref. 2; ACI52750)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        23
FT                   /note="R -> K (in Ref. 2; ACI52750)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   167 AA;  18818 MW;  86F6C1B4283C504E CRC64;
     MTDAADLPYR RNVGAMLFNA QGRILIGRRT DQPGAGGPLD GGVWQCPQGG IDADEDPEEA
     VLRELREEIG TDRAVIMGAR PDWLTYDLPA ALIGRALGGR YRGQTQKWFA LRFTGQDSDI
     RLDDQQPPEF DAWQWIDLPS LPERNVGFKR DIYRTLVRDF ARFSQPA