IPYR2_YEAST
ID IPYR2_YEAST Reviewed; 310 AA.
AC P28239; D6W093;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Inorganic pyrophosphatase, mitochondrial;
DE EC=3.6.1.1 {ECO:0000305|PubMed:1648084};
DE AltName: Full=Pyrophosphate phospho-hydrolase;
DE Short=PPase;
DE Flags: Precursor;
GN Name=PPA2; Synonyms=IPP2; OrderedLocusNames=YMR267W; ORFNames=YM8156.09;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=1648084; DOI=10.1016/s0021-9258(18)98875-7;
RA Lundin M., Baltscheffsky H., Ronne H.;
RT "Yeast PPA2 gene encodes a mitochondrial inorganic pyrophosphatase that is
RT essential for mitochondrial function.";
RL J. Biol. Chem. 266:12168-12172(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP 3D-STRUCTURE MODELING.
RX PubMed=1321599; DOI=10.1016/s0006-291x(05)80783-1;
RA Vihinen M., Lundin M., Baltscheffsky H.;
RT "Computer modeling of two inorganic pyrophosphatases.";
RL Biochem. Biophys. Res. Commun. 186:122-128(1992).
CC -!- FUNCTION: Involved in energy production. Its activity is stimulated by
CC uncouplers of ATP synthesis. {ECO:0000269|PubMed:1648084}.
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:0000305|PubMed:1648084};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24577;
CC Evidence={ECO:0000305|PubMed:1648084};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer that binds non-covalently to a protein complex in
CC the inner mitochondrial membrane. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- MISCELLANEOUS: Present with 195 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PPase family. {ECO:0000305}.
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DR EMBL; M81880; AAA34893.1; -; Genomic_DNA.
DR EMBL; Z49260; CAA89250.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10167.1; -; Genomic_DNA.
DR PIR; A40867; A40867.
DR RefSeq; NP_013994.1; NM_001182774.1.
DR AlphaFoldDB; P28239; -.
DR SMR; P28239; -.
DR BioGRID; 35445; 418.
DR DIP; DIP-1522N; -.
DR IntAct; P28239; 6.
DR MINT; P28239; -.
DR STRING; 4932.YMR267W; -.
DR MaxQB; P28239; -.
DR PaxDb; P28239; -.
DR PRIDE; P28239; -.
DR EnsemblFungi; YMR267W_mRNA; YMR267W; YMR267W.
DR GeneID; 855309; -.
DR KEGG; sce:YMR267W; -.
DR SGD; S000004880; PPA2.
DR VEuPathDB; FungiDB:YMR267W; -.
DR eggNOG; KOG1626; Eukaryota.
DR GeneTree; ENSGT00390000017004; -.
DR HOGENOM; CLU_040684_0_1_1; -.
DR InParanoid; P28239; -.
DR OMA; DWKILCI; -.
DR BioCyc; YEAST:YMR267W-MON; -.
DR Reactome; R-SCE-379716; Cytosolic tRNA aminoacylation.
DR Reactome; R-SCE-71737; Pyrophosphate hydrolysis.
DR PRO; PR:P28239; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P28239; protein.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IMP:SGD.
DR GO; GO:0004427; F:inorganic diphosphatase activity; IMP:SGD.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0009060; P:aerobic respiration; IMP:SGD.
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 1: Evidence at protein level;
KW Hydrolase; Magnesium; Metal-binding; Mitochondrion; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 31..310
FT /note="Inorganic pyrophosphatase, mitochondrial"
FT /id="PRO_0000025413"
FT BINDING 152
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 310 AA; 35573 MW; 985F6E9BDD50BA25 CRC64;
MNLLRMNALT SKARSIERLK QTLNILSIRN HRQFSTIQQG SKYTLGFKKY LTLLNGEVGS
FFHDVPLDLN EHEKTVNMIV EVPRWTTGKF EISKELRFNP IVQDTKNGKL RFVNNIFPYH
GYIHNYGAIP QTWEDPTIEH KLGKCDVALK GDNDPLDCCE IGSDVLEMGS IKKVKVLGSL
ALIDDGELDW KVIVIDVNDP LSSKIDDLEK IEEYFPGILD TTREWFRKYK VPAGKPLNSF
AFHEQYQNSN KTIQTIKKCH NSWKNLISGS LQEKYDNLPN TERAGNGVTL EDSVKPPSQI
PPEVQKWYYV
