IPYR_PICPA
ID IPYR_PICPA Reviewed; 285 AA.
AC O13505;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Inorganic pyrophosphatase;
DE EC=3.6.1.1;
DE AltName: Full=Pyrophosphate phospho-hydrolase;
DE Short=PPase;
GN Name=IPP1;
OS Komagataella pastoris (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=4922;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 76273 / CBS 7435 / CECT 11407 / NRRL Y-11430;
RX PubMed=9818724;
RX DOI=10.1002/(sici)1097-0061(19980630)14:9<861::aid-yea276>3.0.co;2-n;
RA Cosano I.C., Alvarez P., Molina M., Nombela C.;
RT "Cloning and sequence analysis of the Pichia pastoris TRP1, IPP1 and HIS3
RT genes.";
RL Yeast 14:861-867(1998).
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the PPase family. {ECO:0000305}.
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DR EMBL; AJ001000; CAA04453.1; -; Genomic_DNA.
DR AlphaFoldDB; O13505; -.
DR SMR; O13505; -.
DR PRIDE; O13505; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004427; F:inorganic diphosphatase activity; IEA:UniProtKB-EC.
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 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Magnesium; Metal-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..285
FT /note="Inorganic pyrophosphatase"
FT /id="PRO_0000137585"
FT BINDING 79
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
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"
SQ SEQUENCE 285 AA; 32068 MW; 07FB12CE1E6CD47F CRC64;
MSYSTRQIGA ANTLENRVFI EKDGQVVSPF HDIPLYADES KKVLNMVVEV PRWTNAKLEI
SKEEKLNPIL QDTKKGKLRF VRNCFPHHGY IHNYGAFPQT WEDPNVTHPE TKAKGDNDPL
DVCEIGERSY TGQVKQVKVL GVMALLDEGE TDWKVIVIDI NDPLAPKLND IEDVEKHMPG
LLRATNEWFR IYKIPDGKPE NQFAFSGECK NKKYAEEVIQ ECREAWEKLI FGKTSPGEID
LTNTTLQSTP SFSPSATSAV PTASPAAPAK IDQSIDKWFY ISGSA
