ID   IPYR_CHLMU              Reviewed;         209 AA.
AC   Q9PLF1;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 112.
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=TC_0153;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
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; AE002160; AAF39030.1; -; Genomic_DNA.
DR   PIR; A81736; A81736.
DR   RefSeq; WP_010229535.1; NZ_CP027217.1.
DR   AlphaFoldDB; Q9PLF1; -.
DR   SMR; Q9PLF1; -.
DR   STRING; 243161.TC_0153; -.
DR   EnsemblBacteria; AAF39030; AAF39030; TC_0153.
DR   GeneID; 1245687; -.
DR   KEGG; cmu:TC_0153; -.
DR   eggNOG; COG0221; Bacteria.
DR   HOGENOM; CLU_073198_2_1_0; -.
DR   OMA; DEPTFPG; -.
DR   OrthoDB; 1767807at2; -.
DR   Proteomes; UP000000800; Chromosome.
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.
DR   PROSITE; PS00387; PPASE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Magnesium; Metal-binding.
FT   CHAIN           1..209
FT                   /note="Inorganic pyrophosphatase"
FT                   /id="PRO_0000137490"
FT   BINDING         38
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT   BINDING         52
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT   BINDING         64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT   BINDING         92
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT   BINDING         97
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT   BINDING         97
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT   BINDING         130
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT   BINDING         167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
SQ   SEQUENCE   209 AA;  23310 MW;  5DEC1B71801AF81D CRC64;
     MSKTPLSIVH PWHGPVLTRD DYESLCCYIE ITPSDSVKFE LDKETGLLKV DRPQKFSNFC
     PCLYGLLPKT YCGDLSGEYS GQQSNRDNIK GDGDPLDICV LTEKNITQGN ILLQARPIGG
     IRILDSGEAD DKIIAVLEDD LVYGAMEDIS DCPGSVLDMI QHYFLTYKAT PESLIQAKPA
     KIEIIGLYGK KEAQKVIRLA HEDYCNLFM