ID   IPYR_SOLTU              Reviewed;         211 AA.
AC   Q43187;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Soluble inorganic pyrophosphatase PPA1 {ECO:0000303|PubMed:10092174};
DE            EC=3.6.1.1 {ECO:0000269|PubMed:8552717};
DE   AltName: Full=Pyrophosphate phospho-hydrolase {ECO:0000303|PubMed:8552717};
DE            Short=PPase {ECO:0000303|PubMed:8552717};
GN   Name=PPA1 {ECO:0000303|PubMed:10092174};
GN   Synonyms=PPA {ECO:0000303|PubMed:8552717};
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND
RP   ACTIVITY REGULATION.
RC   STRAIN=cv. Desiree;
RX   PubMed=8552717; DOI=10.1104/pp.109.3.853;
RA   du Jardin P., Rojas-Beltran J., Gebhardt C., Brasseur R.;
RT   "Molecular cloning and characterization of a soluble inorganic
RT   pyrophosphatase in potato.";
RL   Plant Physiol. 109:853-860(1995).
RN   [2]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=cv. Desiree;
RX   PubMed=10092174; DOI=10.1023/a:1006136624210;
RA   Rojas-Beltran J.A., Dubois F., Mortiaux F., Portetelle D., Gebhardt C.,
RA   Sangwan R.S., du Jardin P.;
RT   "Identification of cytosolic Mg2+-dependent soluble inorganic
RT   pyrophosphatases in potato and phylogenetic analysis.";
RL   Plant Mol. Biol. 39:449-461(1999).
CC   -!- FUNCTION: Catalyzes the irreversible hydrolysis of pyrophosphate (PPi)
CC       to phosphate. {ECO:0000269|PubMed:8552717}.
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:0000269|PubMed:8552717};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:8552717};
CC   -!- ACTIVITY REGULATION: Strongly inhibited by Ca(2+).
CC       {ECO:0000269|PubMed:8552717}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10092174}.
CC   -!- MISCELLANEOUS: At least 2 separate genes code for soluble
CC       pyrophosphatases in potato. This protein is probably encoded by the
CC       Ppa1(a) locus located on chromosome 12. {ECO:0000305|PubMed:8552717}.
CC   -!- SIMILARITY: Belongs to the PPase family. {ECO:0000305}.
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DR   EMBL; Z36894; CAA85362.1; -; mRNA.
DR   PIR; T07594; T07594.
DR   AlphaFoldDB; Q43187; -.
DR   SMR; Q43187; -.
DR   STRING; 4113.PGSC0003DMT400012843; -.
DR   eggNOG; KOG1626; Eukaryota.
DR   InParanoid; Q43187; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; Q43187; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004427; F:inorganic diphosphatase activity; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR   GO; GO:0071344; P:diphosphate metabolic process; IDA:UniProtKB.
DR   GO; GO:0006796; P:phosphate-containing compound metabolic process; IBA:GO_Central.
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   Cytoplasm; Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..211
FT                   /note="Soluble inorganic pyrophosphatase PPA1"
FT                   /id="PRO_0000137578"
FT   ACT_SITE        83
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P00817"
FT   BINDING         61
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WI55"
FT   BINDING         75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WI55"
FT   BINDING         87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WI55"
FT   BINDING         97
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P0A7A9"
FT   BINDING         102
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P0A7A9"
FT   BINDING         102
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0A7A9"
FT   BINDING         134
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P0A7A9"
FT   BINDING         171
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WI55"
SQ   SEQUENCE   211 AA;  24262 MW;  D06115FC6F2AC22A CRC64;
     MSNENDDLSP QRRAPRLNER ILSSISRRSV AAHPWHDLEI GPEAPSVFNV VIEISKGSKV
     KYELDKKTGL IKVDRILYSS VVYPQNYGFI PRTLCEDNDP MDVLVLMQEP VLPGCFLRAR
     AIGLMPMIDQ GEKDDKIIAV CADDPEYRHY TDIKQLPPHR LAEIRRFFED YKKNENKDVA
     VDDFLPPNSA VNAIQYSMDL YAEYILHSLR K