IPYR4_ARATH
ID IPYR4_ARATH Reviewed; 216 AA.
AC Q9LFF9; Q8LA73;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Soluble inorganic pyrophosphatase 4 {ECO:0000303|PubMed:15135060};
DE EC=3.6.1.1 {ECO:0000269|Ref.6};
DE AltName: Full=Pyrophosphate phospho-hydrolase 4 {ECO:0000303|PubMed:15135060};
DE Short=PPase 4 {ECO:0000303|PubMed:15135060};
GN Name=PPA4 {ECO:0000303|PubMed:15135060};
GN OrderedLocusNames=At3g53620 {ECO:0000312|Araport:AT3G53620};
GN ORFNames=F4P12.320 {ECO:0000312|EMBL:CAB67669.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES,
RP COFACTOR, ACTIVITY REGULATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
CC -!- FUNCTION: Catalyzes the irreversible hydrolysis of pyrophosphate (PPi)
CC to phosphate. The MgPPi(2-) complex binds to the enzyme only after a
CC free Mg(2+) ion has bound. No activity with glycerol-3-phosphate,
CC glucose-6-phosphate, p-nitrophenylphosphate, ADP, NADP(+), NAD(+),NADH,
CC NADPH or phosphoribosyl pyrophosphate as substrates.
CC {ECO:0000269|Ref.6}.
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; Evidence={ECO:0000269|Ref.6};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|Ref.6};
CC -!- ACTIVITY REGULATION: Inhibited by Zn(2+), Ca(2+), Ba(2+), Fe(2+),
CC Co(2+), Cu(2+), Eu(2+), Eu(3+) and Mn(2+). {ECO:0000269|Ref.6}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=kcat is 9.20 sec(-1) for pyrophosphate. {ECO:0000269|Ref.6};
CC -!- SUBUNIT: Monomer. {ECO:0000269|Ref.6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q93V56}.
CC -!- TISSUE SPECIFICITY: Ubiquitous, excepted in pollen. Very low expression
CC in cork, xylem and hypocotyls. {ECO:0000303|Ref.6}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout plant development, with a
CC lower expression in young plantes and a maximum during flowering.
CC {ECO:0000303|Ref.6}.
CC -!- SIMILARITY: Belongs to the PPase family. {ECO:0000305}.
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DR EMBL; AL132966; CAB67669.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79120.1; -; Genomic_DNA.
DR EMBL; AK226578; BAE98700.1; -; mRNA.
DR EMBL; AY087991; AAM65537.1; -; mRNA.
DR PIR; T45902; T45902.
DR RefSeq; NP_190930.1; NM_115222.3.
DR AlphaFoldDB; Q9LFF9; -.
DR SMR; Q9LFF9; -.
DR STRING; 3702.AT3G53620.1; -.
DR iPTMnet; Q9LFF9; -.
DR PaxDb; Q9LFF9; -.
DR PRIDE; Q9LFF9; -.
DR ProteomicsDB; 247044; -.
DR EnsemblPlants; AT3G53620.1; AT3G53620.1; AT3G53620.
DR GeneID; 824530; -.
DR Gramene; AT3G53620.1; AT3G53620.1; AT3G53620.
DR KEGG; ath:AT3G53620; -.
DR Araport; AT3G53620; -.
DR TAIR; locus:2084066; AT3G53620.
DR eggNOG; KOG1626; Eukaryota.
DR HOGENOM; CLU_073198_2_1_1; -.
DR InParanoid; Q9LFF9; -.
DR OMA; VFILREC; -.
DR OrthoDB; 1429691at2759; -.
DR PhylomeDB; Q9LFF9; -.
DR PRO; PR:Q9LFF9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LFF9; baseline and differential.
DR Genevisible; Q9LFF9; 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: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 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Magnesium; Metal-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..216
FT /note="Soluble inorganic pyrophosphatase 4"
FT /id="PRO_0000431797"
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 MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT CONFLICT 119
FT /note="G -> A (in Ref. 4; AAM65537)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 216 AA; 24576 MW; 22F4F41FCCB0E5E5 CRC64;
MAPPIEVSTK SYVEKHVSLP TLNERILSSM SHRSVAAHPW HDLEIGPEAP IIFNCVVEIG
KGSKVKYELD KTTGLIKVDR ILYSSVVYPH NYGFIPRTLC EDSDPIDVLV IMQEPVIPGC
FLRAKAIGLM PMIDQGEKDD KIIAVCADDP EYRHYNDISE LPPHRMAEIR RFFEDYKKNE
NKEVAVNDFL PATAAYDAVQ HSMDLYADYV VENLRR
