ID   IPYR1_CHLRE             Reviewed;         280 AA.
AC   Q93Y52;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Soluble inorganic pyrophosphatase 1, chloroplastic;
DE            EC=3.6.1.1;
DE   AltName: Full=Pyrophosphate phospho-hydrolase 1;
DE            Short=PPase 1;
DE   Flags: Precursor;
GN   Name=ppa1; Synonyms=ppaI;
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAC42762.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   STRAIN=21gr / CC-1690;
RX   PubMed=16313235; DOI=10.1042/bj20051657;
RA   Gomez-Garcia M.R., Losada M., Serrano A.;
RT   "A novel subfamily of monomeric inorganic pyrophosphatases in
RT   photosynthetic eukaryotes.";
RL   Biochem. J. 395:211-221(2006).
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         Evidence={ECO:0000269|PubMed:16313235};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P00817};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=10.5 uM for Mg2-PPi {ECO:0000269|PubMed:16313235};
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|PubMed:16313235};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16313235}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:16313235}.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:16313235}.
CC   -!- MASS SPECTROMETRY: Mass=29850; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16313235};
CC   -!- SIMILARITY: Belongs to the PPase family. {ECO:0000255}.
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DR   EMBL; AJ298231; CAC42762.1; -; mRNA.
DR   RefSeq; XP_001702577.1; XM_001702525.1.
DR   AlphaFoldDB; Q93Y52; -.
DR   SMR; Q93Y52; -.
DR   STRING; 3055.EDP06356; -.
DR   ProMEX; Q93Y52; -.
DR   EnsemblPlants; PNW77146; PNW77146; CHLRE_10g424100v5.
DR   GeneID; 5728217; -.
DR   Gramene; PNW77146; PNW77146; CHLRE_10g424100v5.
DR   KEGG; cre:CHLRE_10g424100v5; -.
DR   eggNOG; KOG1626; Eukaryota.
DR   HOGENOM; CLU_040684_0_0_1; -.
DR   OMA; TLEHRIF; -.
DR   OrthoDB; 1398991at2759; -.
DR   BRENDA; 3.6.1.1; 1318.
DR   SABIO-RK; Q93Y52; -.
DR   GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR   GO; GO:0004427; F:inorganic diphosphatase activity; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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   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   1: Evidence at protein level;
KW   Chloroplast; Hydrolase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000305"
FT   CHAIN           ?..280
FT                   /note="Soluble inorganic pyrophosphatase 1, chloroplastic"
FT                   /id="PRO_0000253938"
FT   BINDING         120
FT                   /ligand="diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:33019"
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P00817"
FT   BINDING         157
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P00817"
FT   BINDING         157
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P00817"
FT   BINDING         189
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P00817"
SQ   SEQUENCE   280 AA;  31134 MW;  5D952A188644BC43 CRC64;
     MALAIRSSLR AAAMGRKAFR QAVPVRVAPA QRVRSVTTAS AEITAYSVEE KGPKDSLEYR
     MFFKQGAKEV SCWHEIPLYA GDGHLHYICE IPKETSAKME VATDEPRTPI KQDVKKGKLR
     FYPYNINWNY GMLPQTWEDP GHTDATLGAA GDNDPVDVVE IGAAAAKRGG VYKVKPVGVL
     AMIDDGELDW KVIAISADDP KAALCNDVED VEKHFPGEIQ KVLEWFRDYK IPDGKPANKF
     GYDNKCMNKE FTLNVIKETH EAYVKLKSGA RANSEELSLI