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IPYR_ORYSJ
ID   IPYR_ORYSJ              Reviewed;         214 AA.
AC   Q0DYB1; O22537; Q6YVH9; Q9ZSU9;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Soluble inorganic pyrophosphatase;
DE            EC=3.6.1.1;
DE   AltName: Full=Pyrophosphate phospho-hydrolase;
DE            Short=PPase;
GN   Name=IPP; OrderedLocusNames=Os02g0704900, LOC_Os02g47600;
GN   ORFNames=OsJ_007809, P0724B10.39;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Ilpoom; TISSUE=Leaf;
RA   Lee J.-S.;
RT   "Molecular cloning and characterization of inorganic pyrophosphatase in
RT   rice.";
RL   Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
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.
CC   -!- SIMILARITY: Belongs to the PPase family. {ECO:0000305}.
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DR   EMBL; AF093629; AAC78101.1; -; mRNA.
DR   EMBL; AP005825; BAD08086.1; -; Genomic_DNA.
DR   EMBL; AP008208; BAF09777.1; -; Genomic_DNA.
DR   EMBL; AP014958; BAS80505.1; -; Genomic_DNA.
DR   EMBL; CM000139; EAZ24326.1; -; Genomic_DNA.
DR   RefSeq; XP_015625137.1; XM_015769651.1.
DR   AlphaFoldDB; Q0DYB1; -.
DR   SMR; Q0DYB1; -.
DR   STRING; 4530.OS02T0704900-02; -.
DR   PaxDb; Q0DYB1; -.
DR   PRIDE; Q0DYB1; -.
DR   EnsemblPlants; Os02t0704900-01; Os02t0704900-01; Os02g0704900.
DR   EnsemblPlants; Os02t0704900-02; Os02t0704900-02; Os02g0704900.
DR   GeneID; 4330457; -.
DR   Gramene; Os02t0704900-01; Os02t0704900-01; Os02g0704900.
DR   Gramene; Os02t0704900-02; Os02t0704900-02; Os02g0704900.
DR   KEGG; osa:4330457; -.
DR   eggNOG; KOG1626; Eukaryota.
DR   HOGENOM; CLU_073198_2_1_1; -.
DR   InParanoid; Q0DYB1; -.
DR   OMA; DEPTFPG; -.
DR   OrthoDB; 1429691at2759; -.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000007752; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
DR   ExpressionAtlas; Q0DYB1; baseline and differential.
DR   Genevisible; Q0DYB1; OS.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004427; F:inorganic diphosphatase activity; IBA:GO_Central.
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   HAMAP; MF_00209; Inorganic_PPase; 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   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..214
FT                   /note="Soluble inorganic pyrophosphatase"
FT                   /id="PRO_0000137577"
FT   BINDING         64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WI55"
FT   BINDING         78
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WI55"
FT   BINDING         90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WI55"
FT   BINDING         100
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         137
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         174
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WI55"
FT   CONFLICT        148
FT                   /note="P -> L (in Ref. 1; AAC78101)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        161
FT                   /note="P -> L (in Ref. 1; AAC78101)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   214 AA;  24160 MW;  9986B4D0DC5ACCB3 CRC64;
     MAGEADGKAP LGSRYPPAAL NERILSSMSQ KHVAAHPWHD LEIGPGAPAV FNCVVEIPRG
     SKVKYELDKA TGLIKVDRVL YSSVVYPHNY GFIPRTLCED GDPMDVLVLM QEQVVPGCFL
     RARAIGLMPM IDQGEKDDKI IAVCADDPEY RHFRDIKEIP PHRLQEIRRF FEDYKKNENK
     EVAVNEFLPA EDAINAIKYS MDLYGAYIIE SLRK
 
 
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