ID   IPYR2_CHLRE             Reviewed;         192 AA.
AC   Q949J1;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Soluble inorganic pyrophosphatase 2;
DE            EC=3.6.1.1;
DE   AltName: Full=Pyrophosphate phospho-hydrolase 2;
DE            Short=PPase 2;
GN   Name=ppa2; Synonyms=ppaII;
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:CAC42763.1}
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:P0A7A9};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=65.2 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: Mitochondrion {ECO:0000269|PubMed:16313235}.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:16313235}.
CC   -!- MASS SPECTROMETRY: Mass=24350; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16313235};
CC   -!- SIMILARITY: Belongs to the PPase family. {ECO:0000255}.
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DR   EMBL; AJ298232; CAC42763.1; -; mRNA.
DR   RefSeq; XP_001694912.1; XM_001694860.1.
DR   AlphaFoldDB; Q949J1; -.
DR   SMR; Q949J1; -.
DR   STRING; 3055.EDP02064; -.
DR   PRIDE; Q949J1; -.
DR   ProMEX; Q949J1; -.
DR   EnsemblPlants; PNW78720; PNW78720; CHLRE_09g387875v5.
DR   GeneID; 5720576; -.
DR   Gramene; PNW78720; PNW78720; CHLRE_09g387875v5.
DR   KEGG; cre:CHLRE_09g387875v5; -.
DR   eggNOG; KOG1626; Eukaryota.
DR   HOGENOM; CLU_073198_2_1_1; -.
DR   OMA; RNKYVMD; -.
DR   OrthoDB; 1429691at2759; -.
DR   BRENDA; 3.6.1.1; 1318.
DR   SABIO-RK; Q949J1; -.
DR   GO; GO:0005739; C:mitochondrion; 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   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   1: Evidence at protein level;
KW   Hydrolase; Magnesium; Metal-binding; Mitochondrion.
FT   CHAIN           1..192
FT                   /note="Soluble inorganic pyrophosphatase 2"
FT                   /id="PRO_0000253939"
FT   BINDING         38
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WI55"
FT   BINDING         52
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WI55"
FT   BINDING         64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WI55"
FT   BINDING         74
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P0A7A9"
FT   BINDING         79
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P0A7A9"
FT   BINDING         79
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0A7A9"
FT   BINDING         111
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P0A7A9"
FT   BINDING         148
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WI55"
SQ   SEQUENCE   192 AA;  22175 MW;  A1CA190C3C3FE597 CRC64;
     MSFYRGTASH PWHDLHPGND APNFVSCVIE IPRGSKVKYE LDKDTGLCFV DRILYSSVVY
     PHNYGFVPKT LCEDGDPLDV LVLMQEPVVP MCFLRAKPIG VMQMLDQGER DDKLIAVHAD
     DPEYKGFTDI SQLPPHRLAE IKRFFEDYKK NEHKEVVVDD FLGAEEAKKV VKDSLNMYQE
     HYVPRKLRNV YE