ID   PPAX_BACCQ              Reviewed;         216 AA.
AC   B9J4R5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Pyrophosphatase PpaX {ECO:0000255|HAMAP-Rule:MF_01250};
DE            EC=3.6.1.1 {ECO:0000255|HAMAP-Rule:MF_01250};
GN   Name=ppaX {ECO:0000255|HAMAP-Rule:MF_01250}; OrderedLocusNames=BCQ_4982;
OS   Bacillus cereus (strain Q1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=361100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Q1;
RX   PubMed=19060151; DOI=10.1128/jb.01629-08;
RA   Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X.,
RA   Xue Y., Zhu Y., Jin Q.;
RT   "Complete genome sequence of the extremophilic Bacillus cereus strain Q1
RT   with industrial applications.";
RL   J. Bacteriol. 191:1120-1121(2009).
CC   -!- FUNCTION: Hydrolyzes pyrophosphate formed during P-Ser-HPr
CC       dephosphorylation by HPrK/P. Might play a role in controlling the
CC       intracellular pyrophosphate pool. {ECO:0000255|HAMAP-Rule:MF_01250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:43474; EC=3.6.1.1; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01250};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01250};
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. PpaX family.
CC       {ECO:0000255|HAMAP-Rule:MF_01250}.
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DR   EMBL; CP000227; ACM15382.1; -; Genomic_DNA.
DR   RefSeq; WP_000700963.1; NC_011969.1.
DR   AlphaFoldDB; B9J4R5; -.
DR   SMR; B9J4R5; -.
DR   EnsemblBacteria; ACM15382; ACM15382; BCQ_4982.
DR   KEGG; bcq:BCQ_4982; -.
DR   HOGENOM; CLU_045011_19_3_9; -.
DR   OMA; LLIFDWD; -.
DR   Proteomes; UP000000441; Chromosome.
DR   GO; GO:0004427; F:inorganic diphosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.150.240; -; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   HAMAP; MF_01250; Pyrophosphat_PpaX; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006439; HAD-SF_hydro_IA.
DR   InterPro; IPR006549; HAD-SF_hydro_IIIA.
DR   InterPro; IPR041492; HAD_2.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR023198; PGP-like_dom2.
DR   InterPro; IPR023733; Pyrophosphatase_Ppax.
DR   Pfam; PF13419; HAD_2; 1.
DR   PRINTS; PR00413; HADHALOGNASE.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
DR   TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
DR   TIGRFAMs; TIGR01662; HAD-SF-IIIA; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium.
FT   CHAIN           1..216
FT                   /note="Pyrophosphatase PpaX"
FT                   /id="PRO_1000165085"
FT   ACT_SITE        9
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01250"
SQ   SEQUENCE   216 AA;  24699 MW;  E0285BB4D9B2BB4E CRC64;
     MKINTVLFDL DGTLINTNEL IISSFLHTLN TYYPDQYKRE DVLPFIGPSL HDTFSKIDES
     KVEELITSYR QFNHDHHDEL VEEYETVYET VQELKKQGYK VGIVTTKARQ TVEMGLKLSK
     LDEFFDVVVT IDDVEHVKPH PEPLQKALQL LDAKPEEALM VGDNHHDIVG GQNAGTKTAA
     VSWTLKGRAY LEAYKPDFML DKMSDLLPIL SDMNRS