IPYR6_ARATH
ID IPYR6_ARATH Reviewed; 300 AA.
AC Q9LXC9; Q8LBD6;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Soluble inorganic pyrophosphatase 6, chloroplastic {ECO:0000303|PubMed:15135060};
DE EC=3.6.1.1 {ECO:0000269|PubMed:15135060};
DE AltName: Full=Inorganic pyrophosphatase 6;
DE AltName: Full=Pyrophosphate phospho-hydrolase 6 {ECO:0000303|PubMed:15135060};
DE Short=PPase 6 {ECO:0000303|PubMed:15135060};
DE Flags: Precursor;
GN Name=PPA6 {ECO:0000303|PubMed:15135060};
GN Synonyms=PPA {ECO:0000312|EMBL:CAC19853.1};
GN OrderedLocusNames=At5g09650 {ECO:0000312|Araport:AT5G09650};
GN ORFNames=F17I14.160 {ECO:0000312|EMBL:CAB89365.1};
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], CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP INDUCTION, 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=16313235; DOI=10.1042/bj20051657;
RA Gomez-Garcia M.R., Losada M., Serrano A.;
RT "A novel subfamily of monomeric inorganic pyrophosphatases in
RT photosynthetic eukaryotes.";
RL Biochem. J. 395:211-221(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia {ECO:0000269|PubMed:10470850};
RX PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
RN [4] {ECO:0000312|EMBL:CAB89365.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia {ECO:0000269|PubMed:11130714};
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [5] {ECO:0000312|EMBL:AAM64828.1}
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 [6] {ECO:0000312|EMBL:AAK76619.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia {ECO:0000269|PubMed:14593172};
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 [7] {ECO:0000312|EMBL:AAM64828.1}
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 [8]
RP 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).
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|PubMed:15135060,
CC ECO:0000269|PubMed:16313235};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P0A7A9};
CC -!- ACTIVITY REGULATION: Inhibited by NaF. {ECO:0000269|PubMed:15135060}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.6 mM for PPi {ECO:0000269|PubMed:15135060};
CC pH dependence:
CC Optimum pH is 7.5. Activity is extremely low below pH 6.5. Activity
CC decreases slightly at more basic pHs, activity at pH 9.0 was only 10%
CC less than that found at pH 7.5. {ECO:0000269|PubMed:15135060};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:15135060}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested. Highest expression
CC in flowers, leaves and roots. Lower levels of expression in siliques,
CC stems, ovary, stigma and pollen. {ECO:0000269|PubMed:15135060,
CC ECO:0000303|Ref.8}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout plant development, with a
CC lower expression in young plantes and a maximum during flowering.
CC {ECO:0000303|Ref.8}.
CC -!- INDUCTION: By glucose, frustose or sucrose at 300 mM, but not at 100
CC mM. {ECO:0000269|PubMed:15135060}.
CC -!- SIMILARITY: Belongs to the PPase family. {ECO:0000305}.
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DR EMBL; AY551439; AAS57950.1; -; mRNA.
DR EMBL; AJ252210; CAC19853.1; -; mRNA.
DR EMBL; AB020752; BAB09520.1; -; Genomic_DNA.
DR EMBL; AL353994; CAB89365.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91421.1; -; Genomic_DNA.
DR EMBL; AY045945; AAK76619.1; -; mRNA.
DR EMBL; AY079355; AAL85086.1; -; mRNA.
DR EMBL; AY087275; AAM64828.1; -; mRNA.
DR PIR; T49933; T49933.
DR RefSeq; NP_196527.1; NM_121002.3.
DR AlphaFoldDB; Q9LXC9; -.
DR SMR; Q9LXC9; -.
DR BioGRID; 16102; 2.
DR IntAct; Q9LXC9; 1.
DR STRING; 3702.AT5G09650.1; -.
DR iPTMnet; Q9LXC9; -.
DR MetOSite; Q9LXC9; -.
DR SwissPalm; Q9LXC9; -.
DR PaxDb; Q9LXC9; -.
DR PRIDE; Q9LXC9; -.
DR ProteomicsDB; 247221; -.
DR EnsemblPlants; AT5G09650.1; AT5G09650.1; AT5G09650.
DR GeneID; 830824; -.
DR Gramene; AT5G09650.1; AT5G09650.1; AT5G09650.
DR KEGG; ath:AT5G09650; -.
DR Araport; AT5G09650; -.
DR TAIR; locus:2144766; AT5G09650.
DR eggNOG; KOG1626; Eukaryota.
DR HOGENOM; CLU_040684_0_0_1; -.
DR InParanoid; Q9LXC9; -.
DR OMA; TLEHRIF; -.
DR OrthoDB; 1398991at2759; -.
DR PhylomeDB; Q9LXC9; -.
DR BRENDA; 3.6.1.1; 399.
DR PRO; PR:Q9LXC9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LXC9; baseline and differential.
DR Genevisible; Q9LXC9; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0004427; F:inorganic diphosphatase activity; IDA:UniProtKB.
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 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 Chloroplast; Hydrolase; Magnesium; Metal-binding; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..66
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 67..300
FT /note="Soluble inorganic pyrophosphatase 6, chloroplastic"
FT /id="PRO_0000253937"
FT ACT_SITE 142
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P00817"
FT BINDING 140
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000250|UniProtKB:P00817"
FT BINDING 173
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="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0A7A9"
FT BINDING 178
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0A7A9"
FT BINDING 210
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0A7A9"
FT CONFLICT 194
FT /note="K -> N (in Ref. 7; AAM64828)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="K -> R (in Ref. 7; AAM64828)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 300 AA; 33380 MW; E5EDA94D56EDD3C4 CRC64;
MAATRVLTAA TAVTQTTSCF LAKQAFTLPA KKSCGGFGGL CFSRRALVLK SKRPFSCSAI
YNPQVKVQEE GPAESLDYRV FFLDGSGKKV SPWHDIPLTL GDGVFNFIVE IPKESKAKME
VATDEDFTPI KQDTKKGKLR YYPYNINWNY GLLPQTWEDP SHANSEVEGC FGDNDPVDVV
EIGETQRKIG DILKIKPLAA LAMIDEGELD WKIVAISLDD PKAHLVNDVE DVEKHFPGTL
TAIRDWFRDY KIPDGKPANR FGLGDKPANK DYALKIIQET NESWAKLVKR SVDAGDLSLY
