ID   PPAX_BACSU              Reviewed;         216 AA.
AC   Q9JMQ2;
DT   13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Pyrophosphatase PpaX;
DE            EC=3.6.1.1;
GN   Name=ppaX; Synonyms=hprP, ptsL, yvoE; OrderedLocusNames=BSU34970;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Lazarevic V., Soldo B., Rivolta C., Reynolds S., Mauel C., Karamata D.;
RT   "Nucleotide sequence of the 300-304 chromosomal segment of Bacillus
RT   subtilis.";
RL   Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   PRELIMINARY FUNCTION.
RX   PubMed=9465101; DOI=10.1073/pnas.95.4.1823;
RA   Galinier A., Kravanja M., Engelmann R., Hengstenberg W., Kilhoffer M.-C.,
RA   Deutscher J., Haiech J.;
RT   "New protein kinase and protein phosphatase families mediate signal
RT   transduction in bacterial catabolite repression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:1823-1828(1998).
RN   [4]
RP   FUNCTION.
RX   PubMed=12359880; DOI=10.1073/pnas.212410399;
RA   Mijakovic I., Poncet S., Galinier A., Monedero V., Fieulaine S., Janin J.,
RA   Nessler S., Marquez J.A., Scheffzek K., Hasenbein S., Hengstenberg W.,
RA   Deutscher J.;
RT   "Pyrophosphate-producing protein dephosphorylation by HPr
RT   kinase/phosphorylase: a relic of early life?";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13442-13447(2002).
RN   [5]
RP   GENE NAME.
RA   Danchin A.;
RL   Submitted (JUL-2004) to UniProtKB.
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:0000269|PubMed:12359880}.
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;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=5.1 uM for pyrophosphate;
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. PpaX family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was originally (PubMed:9465101) called P-Ser-HPr phosphatase
CC       as it has been shown to stimulate P-Ser-HPr dephosphorylation, but
CC       actually (PubMed:12359880) it has pyrophosphatase activity.
CC       {ECO:0000305|PubMed:12359880, ECO:0000305|PubMed:9465101}.
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DR   EMBL; AF017113; AAC67289.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15502.1; -; Genomic_DNA.
DR   PIR; G70044; G70044.
DR   RefSeq; NP_391377.1; NC_000964.3.
DR   RefSeq; WP_003242685.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; Q9JMQ2; -.
DR   SMR; Q9JMQ2; -.
DR   STRING; 224308.BSU34970; -.
DR   jPOST; Q9JMQ2; -.
DR   PaxDb; Q9JMQ2; -.
DR   PRIDE; Q9JMQ2; -.
DR   EnsemblBacteria; CAB15502; CAB15502; BSU_34970.
DR   GeneID; 936613; -.
DR   KEGG; bsu:BSU34970; -.
DR   PATRIC; fig|224308.179.peg.3785; -.
DR   eggNOG; COG0546; Bacteria.
DR   InParanoid; Q9JMQ2; -.
DR   OMA; LLIFDWD; -.
DR   PhylomeDB; Q9JMQ2; -.
DR   BioCyc; BSUB:BSU34970-MON; -.
DR   Proteomes; UP000001570; 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; 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   1: Evidence at protein level;
KW   Hydrolase; Magnesium; Reference proteome.
FT   CHAIN           1..216
FT                   /note="Pyrophosphatase PpaX"
FT                   /id="PRO_0000056839"
FT   ACT_SITE        12
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   216 AA;  24004 MW;  B6B0D47C524289C3 CRC64;
     MSDKQVTTIL FDLDGTLINT NELIIASFLH TLEHYYPSKY KREDVLAFIG PSLFDTFSSM
     DPDKCEDMIA MYRAYNHDMH DSLVTEYETV YETLDALKKA GFTLGIVTTK LRDTVNMGLK
     LTGIGEFFET VVTLDDVTNA KPDPEPVLLA LKQLGSEPAE AIMVGDNYHD VLAGKNAGTK
     TAGVAWTIKG PEMLAKHEPD FMLEKMSDLL QIVGVK