IPYR_SCHPO
ID IPYR_SCHPO Reviewed; 289 AA.
AC P19117;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Inorganic pyrophosphatase;
DE EC=3.6.1.1;
DE AltName: Full=Pyrophosphate phospho-hydrolase;
DE Short=PPase;
GN Name=ppa1; Synonyms=ppa; ORFNames=SPAC23C11.05;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2170949; DOI=10.1093/nar/18.19.5888;
RA Kawasaki I., Adachi N., Ikeda H.;
RT "Nucleotide sequence of S. pombe inorganic pyrophosphatase.";
RL Nucleic Acids Res. 18:5888-5888(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
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 -!- 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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the PPase family. {ECO:0000305}.
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DR EMBL; X54301; CAA38199.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB11158.1; -; Genomic_DNA.
DR PIR; S11496; S11496.
DR RefSeq; NP_593636.1; NM_001019067.2.
DR AlphaFoldDB; P19117; -.
DR SMR; P19117; -.
DR BioGRID; 278494; 5.
DR STRING; 4896.SPAC23C11.05.1; -.
DR iPTMnet; P19117; -.
DR MaxQB; P19117; -.
DR PaxDb; P19117; -.
DR PRIDE; P19117; -.
DR EnsemblFungi; SPAC23C11.05.1; SPAC23C11.05.1:pep; SPAC23C11.05.
DR GeneID; 2542011; -.
DR KEGG; spo:SPAC23C11.05; -.
DR PomBase; SPAC23C11.05; -.
DR VEuPathDB; FungiDB:SPAC23C11.05; -.
DR eggNOG; KOG1626; Eukaryota.
DR HOGENOM; CLU_040684_0_1_1; -.
DR OMA; TLEHRIF; -.
DR PhylomeDB; P19117; -.
DR Reactome; R-SPO-379716; Cytosolic tRNA aminoacylation.
DR Reactome; R-SPO-379726; Mitochondrial tRNA aminoacylation.
DR Reactome; R-SPO-71737; Pyrophosphate hydrolysis.
DR PRO; PR:P19117; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004427; F:inorganic diphosphatase activity; ISO:PomBase.
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 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..289
FT /note="Inorganic pyrophosphatase"
FT /id="PRO_0000137586"
FT BINDING 80
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 289 AA; 32468 MW; 207DB3B652AF0306 CRC64;
MSEYTTREVG ALNTLDYQVY VEKNGTPISS WHDIPLYANA EKTILNMVVE IPRWTQAKLE
ITKEATLNPI KQDTKKGKLR FVRNCFPHHG YIWNYGAFPQ TYEDPNVVHP ETKAKGDSDP
LDVCEIGEAR GYTGQVKQVK VLGVMALLDE GETDWKVIVI DVNDPLAPKL NDIEDVERHM
PGLIRATNEW FRIYKIPDGK PENSFAFSGE CKNRKYAEEV VRECNEAWER LITGKTDAKS
DFSLVNVSVT GSVANDPSVS STIPPAQELA PAPVDPSVHK WFYISGSPL
