ID   IPYR_LEPIC              Reviewed;         178 AA.
AC   Q72MG4;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Inorganic pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00209};
DE            EC=3.6.1.1 {ECO:0000255|HAMAP-Rule:MF_00209};
DE   AltName: Full=Pyrophosphate phospho-hydrolase {ECO:0000255|HAMAP-Rule:MF_00209};
DE            Short=PPase {ECO:0000255|HAMAP-Rule:MF_00209};
GN   Name=ppa {ECO:0000255|HAMAP-Rule:MF_00209}; OrderedLocusNames=LIC_13223;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni
OS   (strain Fiocruz L1-130).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=267671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fiocruz L1-130;
RX   PubMed=15028702; DOI=10.1128/jb.186.7.2164-2172.2004;
RA   Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B.,
RA   Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V.,
RA   Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L.,
RA   Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S., Ferro M.I.T.,
RA   Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H.,
RA   Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M.,
RA   Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L.,
RA   Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A.,
RA   Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A.,
RA   Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A.;
RT   "Comparative genomics of two Leptospira interrogans serovars reveals novel
RT   insights into physiology and pathogenesis.";
RL   J. Bacteriol. 186:2164-2172(2004).
CC   -!- FUNCTION: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi)
CC       forming two phosphate ions. {ECO:0000255|HAMAP-Rule:MF_00209}.
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_00209};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00209};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00209}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00209}.
CC   -!- SIMILARITY: Belongs to the PPase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00209}.
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DR   EMBL; AE016823; AAS71768.1; -; Genomic_DNA.
DR   RefSeq; WP_000233562.1; NC_005823.1.
DR   AlphaFoldDB; Q72MG4; -.
DR   SMR; Q72MG4; -.
DR   PaxDb; Q72MG4; -.
DR   EnsemblBacteria; AAS71768; AAS71768; LIC_13223.
DR   GeneID; 61143089; -.
DR   KEGG; lic:LIC_13223; -.
DR   HOGENOM; CLU_073198_1_2_12; -.
DR   OMA; DEPTFPG; -.
DR   Proteomes; UP000007037; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0006796; P:phosphate-containing compound metabolic process; IEA:InterPro.
DR   CDD; cd00412; pyrophosphatase; 1.
DR   Gene3D; 3.90.80.10; -; 1.
DR   HAMAP; MF_00209; Inorganic_PPase; 1.
DR   InterPro; IPR008162; Pyrophosphatase.
DR   InterPro; IPR036649; Pyrophosphatase_sf.
DR   PANTHER; PTHR10286; PTHR10286; 1.
DR   Pfam; PF00719; Pyrophosphatase; 1.
DR   SUPFAM; SSF50324; SSF50324; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Magnesium; Metal-binding.
FT   CHAIN           1..178
FT                   /note="Inorganic pyrophosphatase"
FT                   /id="PRO_0000137505"
FT   BINDING         31
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT   BINDING         45
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT   BINDING         57
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT   BINDING         67
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT   BINDING         72
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT   BINDING         72
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT   BINDING         104
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT   BINDING         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
SQ   SEQUENCE   178 AA;  20445 MW;  5469743F80AE33D6 CRC64;
     MVHPWHDISP GDQNPEIVNG VIEIKRGSRA KYEVDKEYGI LKLDRVLYSS FYYPANYGFI
     PQSYCGDQDP LDILVLSQVE LEPLCLVKAK VIGVMRMLDS GEEDDKIIAV AANDMSVNHI
     NDISELPPHF TLELKHFFED YKKLENKTVV IEEFQNAILA RKIVLDSLEL YKKTFPKK