IPYR2_ARATH
ID IPYR2_ARATH Reviewed; 218 AA.
AC P21216; Q8L988; Q9ZPV6;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Soluble inorganic pyrophosphatase 2 {ECO:0000303|PubMed:15135060};
DE EC=3.6.1.1 {ECO:0000250|UniProtKB:Q93V56};
DE AltName: Full=Pyrophosphate phospho-hydrolase 2 {ECO:0000303|PubMed:15135060};
DE Short=PPase 2 {ECO:0000303|PubMed:15135060};
GN Name=PPA2 {ECO:0000303|PubMed:15135060};
GN Synonyms=PPA1 {ECO:0000303|PubMed:1654155};
GN OrderedLocusNames=At2g18230 {ECO:0000312|Araport:AT2G18230};
GN ORFNames=T30D6.26 {ECO:0000312|EMBL:AAD15513.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=1654155; DOI=10.1007/bf00020567;
RA Kieber J.J., Signer E.R.;
RT "Cloning and characterization of an inorganic pyrophosphatase gene from
RT Arabidopsis thaliana.";
RL Plant Mol. Biol. 16:345-348(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15135060; DOI=10.1016/j.febslet.2004.03.080;
RA Schulze S., Mant A., Kossmann J., Lloyd J.R.;
RT "Identification of an Arabidopsis inorganic pyrophosphatase capable of
RT being imported into chloroplasts.";
RL FEBS Lett. 565:101-105(2004).
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 Evidence={ECO:0000250|UniProtKB:Q93V56};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P0A7A9};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q93V56}.
CC -!- SIMILARITY: Belongs to the PPase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA40764.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X57545; CAA40764.1; ALT_FRAME; mRNA.
DR EMBL; AC006439; AAD15513.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06742.1; -; Genomic_DNA.
DR EMBL; AY048209; AAK82472.1; -; mRNA.
DR EMBL; AY091698; AAM10297.1; -; mRNA.
DR EMBL; AY088579; AAM66110.1; -; mRNA.
DR PIR; H84561; H84561.
DR PIR; S13379; S13379.
DR RefSeq; NP_179415.1; NM_127380.4.
DR AlphaFoldDB; P21216; -.
DR SMR; P21216; -.
DR BioGRID; 1695; 3.
DR STRING; 3702.AT2G18230.1; -.
DR MetOSite; P21216; -.
DR PaxDb; P21216; -.
DR PRIDE; P21216; -.
DR ProteomicsDB; 247042; -.
DR EnsemblPlants; AT2G18230.1; AT2G18230.1; AT2G18230.
DR GeneID; 816338; -.
DR Gramene; AT2G18230.1; AT2G18230.1; AT2G18230.
DR KEGG; ath:AT2G18230; -.
DR Araport; AT2G18230; -.
DR TAIR; locus:2062195; AT2G18230.
DR eggNOG; KOG1626; Eukaryota.
DR HOGENOM; CLU_073198_2_1_1; -.
DR InParanoid; P21216; -.
DR OMA; DEPTFPG; -.
DR OrthoDB; 1429691at2759; -.
DR PhylomeDB; P21216; -.
DR PRO; PR:P21216; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P21216; baseline and differential.
DR Genevisible; P21216; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005654; C:nucleoplasm; IDA:TAIR.
DR GO; GO:0004427; F:inorganic diphosphatase activity; IGI:TAIR.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0052546; P:cell wall pectin metabolic process; IGI:TAIR.
DR GO; GO:0052386; P:cell wall thickening; IMP:TAIR.
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..218
FT /note="Soluble inorganic pyrophosphatase 2"
FT /id="PRO_0000137574"
FT ACT_SITE 90
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P00817"
FT BINDING 68
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WI55"
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WI55"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WI55"
FT BINDING 104
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0A7A9"
FT BINDING 109
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0A7A9"
FT BINDING 109
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0A7A9"
FT BINDING 141
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0A7A9"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WI55"
FT CONFLICT 12
FT /note="G -> A (in Ref. 5; AAM66110)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="A -> S (in Ref. 5; AAM66110)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="V -> A (in Ref. 1; CAA40764)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 218 AA; 24671 MW; 884DCFAB6B1B239A CRC64;
MAEIKDEGSA KGYAFPLRNP NVTLNERNFA AFTHRSAAAH PWHDLEIGPE APTVFNCVVE
ISKGGKVKYE LDKNSGLIKV DRVLYSSIVY PHNYGFIPRT ICEDSDPMDV LVLMQEPVLT
GSFLRARAIG LMPMIDQGEK DDKIIAVCAD DPEFRHYRDI KELPPHRLAE IRRFFEDYKK
NENKKVDVEA FLPAQAAIDA IKDSMDLYAA YIKAGLQR
