ID   IPYR_HORVV              Reviewed;         215 AA.
AC   O23979;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Soluble inorganic pyrophosphatase;
DE            EC=3.6.1.1;
DE   AltName: Full=Pyrophosphate phospho-hydrolase;
DE            Short=PPase;
GN   Name=IPP;
OS   Hordeum vulgare subsp. vulgare (Domesticated barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=112509;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Triumph;
RX   PubMed=9620271; DOI=10.1023/a:1005931003483;
RA   Visser K., Heimovaara-Dijkstra S., Kijne J.W., Wang M.;
RT   "Molecular cloning and characterization of an inorganic pyrophosphatase
RT   from barley.";
RL   Plant Mol. Biol. 37:131-140(1998).
CC   -!- FUNCTION: May play a role in germination.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Expressed in metabolically active tissue such as
CC       root, shoot, embryo and aleurone.
CC   -!- SIMILARITY: Belongs to the PPase family. {ECO:0000305}.
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DR   EMBL; AF009675; AAC50012.1; -; mRNA.
DR   PIR; T04421; T04421.
DR   AlphaFoldDB; O23979; -.
DR   SMR; O23979; -.
DR   STRING; 112509.O23979; -.
DR   PRIDE; O23979; -.
DR   eggNOG; KOG1626; Eukaryota.
DR   InParanoid; O23979; -.
DR   Proteomes; UP000011116; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004427; F:inorganic diphosphatase activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
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   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   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..215
FT                   /note="Soluble inorganic pyrophosphatase"
FT                   /id="PRO_0000137575"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         103
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         108
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         108
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         140
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   215 AA;  24049 MW;  AA99D00A69CE948D CRC64;
     MSQEDSTSAA AAQQPTSRPA PKLNERILSS LSRRGGGAHP WHDLEIGPGA PAVFNVVVEI
     TKGSKVKYEL DKKTGLIKVD RVLYSSVVYP HNYGFIPRTL CEDNDPMDVL VLMQEPVIPG
     SFLRARAIGL MPMIDQGEKD DKIIAVCADD PEYRHYSTSV SLLPRLQEIK RLEDYKKNEN
     KEVAVDAFLP ATTAREAIQY SMDLYAQYIL QSLRQ