ID   RPPH_BRADU              Reviewed;         167 AA.
AC   Q89X78;
DT   06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 90.
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=blr0436;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(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; BA000040; BAC45701.1; -; Genomic_DNA.
DR   RefSeq; NP_767076.1; NC_004463.1.
DR   RefSeq; WP_011083268.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q89X78; -.
DR   SMR; Q89X78; -.
DR   STRING; 224911.27348684; -.
DR   EnsemblBacteria; BAC45701; BAC45701; BAC45701.
DR   GeneID; 64020294; -.
DR   KEGG; bja:blr0436; -.
DR   PATRIC; fig|224911.44.peg.8966; -.
DR   eggNOG; COG1051; Bacteria.
DR   HOGENOM; CLU_087195_3_0_5; -.
DR   InParanoid; Q89X78; -.
DR   OMA; WAAAKRE; -.
DR   PhylomeDB; Q89X78; -.
DR   Proteomes; UP000002526; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0019144; F:ADP-sugar diphosphatase activity; IBA:GO_Central.
DR   GO; GO:0006753; P:nucleoside phosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0019693; P:ribose phosphate metabolic process; IBA:GO_Central.
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; IPR000086; NUDIX_hydrolase_dom.
DR   InterPro; IPR022927; RppH.
DR   Pfam; PF00293; NUDIX; 1.
DR   SUPFAM; SSF55811; SSF55811; 1.
DR   PROSITE; PS51462; NUDIX; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..167
FT                   /note="RNA pyrophosphohydrolase"
FT                   /id="PRO_0000056997"
FT   DOMAIN          8..159
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00298"
FT   MOTIF           47..68
FT                   /note="Nudix box"
SQ   SEQUENCE   167 AA;  19191 MW;  2DDFF55BF9723BA3 CRC64;
     MARYEDLPYR TCVGVMLINA KGLVFIGRRA GGIEHIDDTH VWQMPQGGVD PGEDTWAAAK
     RELYEETSVR SVERLGEVPD WLIYDIPRTV AGRAWKGRYR GQRQKWFAVR FTGKDSEINV
     ENPGGGHKAE FVSWRWEPMK NLPGLIIPFK RPVYERVVKE FSALAEE