IPYR3_ARATH
ID IPYR3_ARATH Reviewed; 216 AA.
AC O82793; Q8GXR0;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Soluble inorganic pyrophosphatase 3 {ECO:0000303|PubMed:15135060};
DE EC=3.6.1.1 {ECO:0000250|UniProtKB:Q93V56};
DE AltName: Full=Pyrophosphate phospho-hydrolase 3 {ECO:0000303|PubMed:15135060};
DE Short=PPase 3 {ECO:0000303|PubMed:15135060};
GN Name=PPA3 {ECO:0000303|PubMed:15135060};
GN OrderedLocusNames=At2g46860 {ECO:0000312|Araport:AT2G46860};
GN ORFNames=F19D11.23 {ECO:0000312|EMBL:AAM15021.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP 3D-STRUCTURE MODELING.
RX PubMed=10413099; DOI=10.1016/s0014-5793(99)00779-6;
RA Sivula T., Salminen A., Parfenyev A.N., Pohjanjoki P., Goldman A.,
RA Cooperman B.S., Baykov A.A., Lahti R.;
RT "Evolutionary aspects of inorganic pyrophosphatase.";
RL FEBS Lett. 454:75-80(1999).
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).
RN [7]
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RA Navarro-De la Sancha E., Coello-Coutino M.P., Valencia-Turcotte L.G.,
RA Hernandez-Dominguez E.E., Trejo-Yepes G., Rodriguez-Sotres R.;
RT "Characterization of two soluble inorganic pyrophosphatases from
RT Arabidopsis thaliana.";
RL Plant Sci. 172:796-807(2007).
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:Q93V56};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q93V56}.
CC -!- TISSUE SPECIFICITY: Expressed preferentially in stamen, pollen and
CC flower, and at a low level in lateral roots and root elongation zones.
CC {ECO:0000303|Ref.7}.
CC -!- SIMILARITY: Belongs to the PPase family. {ECO:0000305}.
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DR EMBL; AC004411; AAC34242.1; -; Genomic_DNA.
DR EMBL; AC005310; AAM15021.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10764.1; -; Genomic_DNA.
DR EMBL; AK118094; BAC42722.1; -; mRNA.
DR EMBL; BT025278; ABF19031.1; -; mRNA.
DR PIR; T02201; T02201.
DR RefSeq; NP_182209.1; NM_130253.3.
DR AlphaFoldDB; O82793; -.
DR SMR; O82793; -.
DR STRING; 3702.AT2G46860.1; -.
DR iPTMnet; O82793; -.
DR PaxDb; O82793; -.
DR PRIDE; O82793; -.
DR ProteomicsDB; 248489; -.
DR EnsemblPlants; AT2G46860.1; AT2G46860.1; AT2G46860.
DR GeneID; 819299; -.
DR Gramene; AT2G46860.1; AT2G46860.1; AT2G46860.
DR KEGG; ath:AT2G46860; -.
DR Araport; AT2G46860; -.
DR TAIR; locus:2041424; AT2G46860.
DR eggNOG; KOG1626; Eukaryota.
DR HOGENOM; CLU_073198_2_1_1; -.
DR InParanoid; O82793; -.
DR OMA; GIMPMID; -.
DR OrthoDB; 1429691at2759; -.
DR PhylomeDB; O82793; -.
DR PRO; PR:O82793; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O82793; baseline and differential.
DR Genevisible; O82793; 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; 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..216
FT /note="Soluble inorganic pyrophosphatase 3"
FT /id="PRO_0000431796"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 88
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P00817"
FT BINDING 66
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WI55"
FT BINDING 80
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WI55"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WI55"
FT BINDING 102
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0A7A9"
FT BINDING 107
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0A7A9"
FT BINDING 107
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0A7A9"
FT BINDING 139
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0A7A9"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WI55"
FT CONFLICT 175
FT /note="D -> N (in Ref. 3; BAC42722)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 216 AA; 24916 MW; 2414341C4860F87B CRC64;
MSEEAYEETQ ESSQSPRPVP KLNERILSTL SRRSVAAHPW HDLEIGPEAP LVFNVVVEIT
KGSKVKYELD KKTGLIKVDR ILYSSVVYPH NYGFIPRTLC EDNDPLDVLV LMQEPVLPGC
FLRARAIGLM PMIDQGEKDD KIIAVCADDP EYKHFTDIKQ LAPHRLQEIR RFFEDYKKNE
NKKVAVNDFL PSESAHEAIQ YSMDLYAEYI LHTLRR
