ID   PPAX_BACCR              Reviewed;         216 AA.
AC   Q815I8;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 101.
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=BC_5162;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
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; AE016877; AAP12027.1; -; Genomic_DNA.
DR   RefSeq; NP_834826.1; NC_004722.1.
DR   RefSeq; WP_001222403.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q815I8; -.
DR   SMR; Q815I8; -.
DR   STRING; 226900.BC_5162; -.
DR   EnsemblBacteria; AAP12027; AAP12027; BC_5162.
DR   GeneID; 67509790; -.
DR   KEGG; bce:BC5162; -.
DR   PATRIC; fig|226900.8.peg.5320; -.
DR   HOGENOM; CLU_045011_19_3_9; -.
DR   OMA; LLIFDWD; -.
DR   Proteomes; UP000001417; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004427; F:inorganic diphosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008967; F:phosphoglycolate phosphatase activity; IBA:GO_Central.
DR   GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..216
FT                   /note="Pyrophosphatase PpaX"
FT                   /id="PRO_0000056836"
FT   ACT_SITE        9
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01250"
SQ   SEQUENCE   216 AA;  24773 MW;  6DC0FB6D3CD12A04 CRC64;
     MRINTVLFDL DGTLINTNEL IISSFLHTLN TYYPNQYKRE DVLPFIGPSL HDTFSKIDES
     KVEEMITSYR EFNHDHHDEL VEEYETVYET VRELKKQGYK VGIVTTKARQ TVEMGLQLSK
     LDEFFDVVVT IDDVEHVKPH PEPLQKALEL LDAKPEEALM VGDNHHDIVG GQNAGTKTAA
     VSWTLKGRAY LEAYKPDFML DKMSDLLPIL SNMNRS