ID   PPAX_CLOPE              Reviewed;         214 AA.
AC   Q8XIY6;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Putative 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=CPE1977;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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; BA000016; BAB81683.1; -; Genomic_DNA.
DR   RefSeq; WP_011010709.1; NC_003366.1.
DR   AlphaFoldDB; Q8XIY6; -.
DR   SMR; Q8XIY6; -.
DR   STRING; 195102.gene:10491246; -.
DR   EnsemblBacteria; BAB81683; BAB81683; BAB81683.
DR   KEGG; cpe:CPE1977; -.
DR   HOGENOM; CLU_045011_19_3_9; -.
DR   OMA; LLIFDWD; -.
DR   Proteomes; UP000000818; 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; 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.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Reference proteome.
FT   CHAIN           1..214
FT                   /note="Putative pyrophosphatase PpaX"
FT                   /id="PRO_0000056840"
FT   ACT_SITE        8
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01250"
SQ   SEQUENCE   214 AA;  24081 MW;  D267087B657D20BE CRC64;
     MIKAVLFDLD GTLINTNDLI LKSFKHTFKT MLDLEPSEEE ITMNYGRPLQ EIFKSYDENR
     IEEMINCYRK INLELHDDEC KEFADVDLML KTLKSKGIKI GVVTSKKSDM AERGAKLMGI
     FKYFDTFITP EITTKHKPDG EPVLKACENL GVSPSEALMV GDSPYDILAG KNAGAKTCGV
     KYTALPLEKL GESNPDFYVD KPLEILDLVE KLNS