ID   PPAX_OCEIH              Reviewed;         214 AA.
AC   Q8ENK3;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-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=OB2479;
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS   3954 / HTE831).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
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; BA000028; BAC14435.1; -; Genomic_DNA.
DR   RefSeq; WP_011066872.1; NC_004193.1.
DR   AlphaFoldDB; Q8ENK3; -.
DR   SMR; Q8ENK3; -.
DR   STRING; 221109.22778165; -.
DR   EnsemblBacteria; BAC14435; BAC14435; BAC14435.
DR   KEGG; oih:OB2479; -.
DR   eggNOG; COG0546; Bacteria.
DR   HOGENOM; CLU_045011_19_3_9; -.
DR   OMA; LLIFDWD; -.
DR   OrthoDB; 1484726at2; -.
DR   PhylomeDB; Q8ENK3; -.
DR   Proteomes; UP000000822; 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   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="Pyrophosphatase PpaX"
FT                   /id="PRO_0000056844"
FT   ACT_SITE        9
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01250"
SQ   SEQUENCE   214 AA;  24442 MW;  34610148DB1A6A40 CRC64;
     MSIRTILFDL DGTLIDTNTL IKASFEHTFK EYNLNFSNEE ILKFNGPPLV DTFNKIDETK
     ADRMITTFRE HNIREHDNFV TAFPHVYDTL EELQNRNISL GIVSTKMRHT VHMGLELTGI
     SKFFSTIITY DDVTHAKPHP EPVQMAMQKL GAHPEHTLMV GDNHHDIVSG QRANVQTAAV
     AWSLKDTNYL KSFHPDYIIE DIKDIITIVG DSFA