IPYR2_SCHPO
ID IPYR2_SCHPO Reviewed; 286 AA.
AC P87118;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Putative inorganic pyrophosphatase C3A12.02;
DE EC=3.6.1.1;
DE AltName: Full=Pyrophosphate phosphohydrolase;
DE Short=PPase;
GN ORFNames=SPAC3A12.02;
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 [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).
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 {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PPase family. {ECO:0000305}.
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DR EMBL; CU329670; CAB08747.1; -; Genomic_DNA.
DR PIR; T38670; T38670.
DR RefSeq; NP_593328.1; NM_001018759.2.
DR AlphaFoldDB; P87118; -.
DR SMR; P87118; -.
DR STRING; 4896.SPAC3A12.02.1; -.
DR MaxQB; P87118; -.
DR PaxDb; P87118; -.
DR PRIDE; P87118; -.
DR EnsemblFungi; SPAC3A12.02.1; SPAC3A12.02.1:pep; SPAC3A12.02.
DR GeneID; 2542957; -.
DR KEGG; spo:SPAC3A12.02; -.
DR PomBase; SPAC3A12.02; -.
DR VEuPathDB; FungiDB:SPAC3A12.02; -.
DR eggNOG; KOG1626; Eukaryota.
DR HOGENOM; CLU_040684_0_1_1; -.
DR InParanoid; P87118; -.
DR OMA; WTQAKCE; -.
DR PhylomeDB; P87118; -.
DR Reactome; R-SPO-379716; Cytosolic tRNA aminoacylation.
DR Reactome; R-SPO-71737; Pyrophosphate hydrolysis.
DR PRO; PR:P87118; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0004427; F:inorganic diphosphatase activity; ISO:PomBase.
DR GO; GO:0000287; F:magnesium ion binding; ISS:PomBase.
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 CHAIN 1..286
FT /note="Putative inorganic pyrophosphatase C3A12.02"
FT /id="PRO_0000137590"
FT BINDING 85
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
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 127
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 286 AA; 32899 MW; FBE4A7EEF9132212 CRC64;
MASLAKNILQ FRSKITGKLN TPDFRVYCYK NNKPISFFHD VPLTSDKDTF NMVTEIPRWT
QAKCEISLTS PFHPIKQDLK NGKLRYVANS FPYHGFIWNY GALPQTWEDP NVIDSRTKMK
GDGDPLDVCE IGGSIGYIGQ IKQVKVLGAL GLIDQGETDW KILAIDINDP RAKLLNDISD
VQNLMPRLLP CTRDWFAIYK IPDGKPKNRF FFDGNYLPKS DALDIIAQCH QHWKVSRDRK
QYIKNFHNES VNNVDLINKI NSLKEEVSQN VSNYPSFPYF HTIPNL
