AC   MF_00209;
DC   Protein; auto
TR   HAMAP; MF_00209; -; 1; level=0
XX
Names: Inorganic_PPase
XX
ID   IPYR
DE   RecName: Full=Inorganic pyrophosphatase;
DE            EC=3.6.1.1;
DE   AltName: Full=Pyrophosphate phospho-hydrolase;
DE            Short=PPase;
GN   Name=ppa;
XX
CC   -!- FUNCTION: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi)
CC       forming two phosphate ions.
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;
CC   -!- SUBUNIT: Homohexamer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the PPase family.
XX
DR   Pfam; PF00719; Pyrophosphatase; 1; trigger=no
DR   PROSITE; PS00387; PPASE; 1; trigger=no
XX
KW   Cytoplasm
KW   Hydrolase
KW   Magnesium
KW   Metal-binding
XX
GO   GO:0004427; F:inorganic diphosphate phosphatase activity
GO   GO:0000287; F:magnesium ion binding
GO   GO:0005737; C:cytoplasm
XX
FT   From: IPYR_MYCTU (P9WI55)
case <OC:Actinomycetota>
FT   ACT_SITE        89
FT                   /note="Proton acceptor"
FT   Condition: D
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT   Condition: E
FT   BINDING         52
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT   Condition: D
FT   BINDING         57
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT   Condition: D
FT   BINDING         57
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT   Condition: D
FT   BINDING         84
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT   Condition: D
FT   BINDING         89
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT   Condition: D
FT   BINDING         89
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT   Condition: D
end case
FT   BINDING         16
FT                   /ligand="substrate"
FT   Condition: K
FT   BINDING         30
FT                   /ligand="substrate"
FT   Condition: R
FT   BINDING         42
FT                   /ligand="substrate"
FT   Condition: Y
FT   BINDING         126
FT                   /ligand="substrate"
FT   Condition: Y
FT   From: IPYR_ECOLI (P0A7A9)
case not <OC:Actinomycetota>
FT   BINDING         66
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT   Condition: D
FT   BINDING         71
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT   Condition: D
FT   BINDING         71
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT   Condition: D
FT   BINDING         103
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT   Condition: D
end case
XX
Size: 158-215;
Related: None;
Template: P0A7A9; P38576; P50308; P80562; P9WI55;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in PSESM
Plasmid: None
Comments: None
XX
# Revision 1.36 2023/01/13
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