PPA26_ARATH
ID PPA26_ARATH Reviewed; 475 AA.
AC Q949Y3; Q5MAU9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Bifunctional purple acid phosphatase 26;
DE Includes:
DE RecName: Full=Acid phosphatase;
DE EC=3.1.3.2;
DE Includes:
DE RecName: Full=Peroxidase;
DE EC=1.11.1.7;
DE Flags: Precursor;
GN Name=PAP26; OrderedLocusNames=At5g34850; ORFNames=T5E15.10;
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], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=16244908; DOI=10.1007/s11103-005-0183-0;
RA Zhu H., Qian W., Lu X., Li D., Liu X., Liu K., Wang D.;
RT "Expression patterns of purple acid phosphatase genes in Arabidopsis organs
RT and functional analysis of AtPAP23 predominantly transcribed in flower.";
RL Plant Mol. Biol. 59:581-594(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
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 [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 PROTEIN SEQUENCE OF 31-53, FUNCTION, GLYCOSYLATION, CHARACTERIZATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16963519; DOI=10.1104/pp.106.087171;
RA Veljanovski V., Vanderbeld B., Knowles V.L., Snedden W.A., Plaxton W.C.;
RT "Biochemical and molecular characterization of AtPAP26, a vacuolar purple
RT acid phosphatase up-regulated in phosphate-deprived Arabidopsis suspension
RT cells and seedlings.";
RL Plant Physiol. 142:1282-1293(2006).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12021284; DOI=10.1074/jbc.m204183200;
RA Li D., Zhu H., Liu K., Liu X., Leggewie G., Udvardi M., Wang D.;
RT "Purple acid phosphatases of Arabidopsis thaliana. Comparative analysis and
RT differential regulation by phosphate deprivation.";
RL J. Biol. Chem. 277:27772-27781(2002).
CC -!- FUNCTION: Metallo-phosphoesterase involved in phosphate metabolism.
CC Acid phosphatase activity with phosphoenolpyruvate, inorganic
CC pyrophosphate, phenyl-phosphate and p-nitrophenyl-phosphate as the most
CC effective substrates. No activity with phytic acid, phosphocholine or
CC bis-p-nitrophenyl-phosphate. Has a peroxidase activity at alkaline pH.
CC {ECO:0000269|PubMed:16963519}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2
CC H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7;
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by Mg(2+), Co(2+), Mn(2+) and Ba(2+).
CC Inhibited by Fe(2+), Cu(2+), Zn(2+), NaF, molybdate, arsenate, vanadate
CC and inorganic phosphate. No effect of tartrate, Asp, Gln, glutathione,
CC Asn, ascorbic acid and phosphite.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=520 nm {ECO:0000269|PubMed:16963519};
CC Kinetic parameters:
CC KM=0.8 mM for phosphoenolpyruvate (for the phosphatase activity)
CC {ECO:0000269|PubMed:16963519};
CC pH dependence:
CC Optimum pH is 5.6 for the phosphatase activity and 8.8 for the
CC peroxidase activity. {ECO:0000269|PubMed:16963519};
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:16963519}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers and
CC siliques. {ECO:0000269|PubMed:16244908}.
CC -!- INDUCTION: Not induced at the transcription level by phosphate
CC starvation, but accumulation of the protein in starved shoots.
CC {ECO:0000269|PubMed:16963519}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:16963519}.
CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. Purple
CC acid phosphatase family. {ECO:0000305}.
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DR EMBL; AY842026; AAW29950.1; -; mRNA.
DR EMBL; AC019013; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93912.1; -; Genomic_DNA.
DR EMBL; AY050812; AAK92747.1; -; mRNA.
DR EMBL; AY091415; AAM14354.1; -; mRNA.
DR RefSeq; NP_198334.1; NM_122874.4.
DR AlphaFoldDB; Q949Y3; -.
DR SMR; Q949Y3; -.
DR STRING; 3702.AT5G34850.1; -.
DR iPTMnet; Q949Y3; -.
DR PaxDb; Q949Y3; -.
DR PRIDE; Q949Y3; -.
DR ProteomicsDB; 249027; -.
DR EnsemblPlants; AT5G34850.1; AT5G34850.1; AT5G34850.
DR GeneID; 833406; -.
DR Gramene; AT5G34850.1; AT5G34850.1; AT5G34850.
DR KEGG; ath:AT5G34850; -.
DR Araport; AT5G34850; -.
DR TAIR; locus:2184657; AT5G34850.
DR eggNOG; KOG1378; Eukaryota.
DR HOGENOM; CLU_013387_0_1_1; -.
DR InParanoid; Q949Y3; -.
DR OMA; GLWYAFT; -.
DR OrthoDB; 426430at2759; -.
DR PhylomeDB; Q949Y3; -.
DR BRENDA; 3.1.3.2; 399.
DR PRO; PR:Q949Y3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q949Y3; baseline and differential.
DR Genevisible; Q949Y3; AT.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; IDA:TAIR.
DR GO; GO:0003993; F:acid phosphatase activity; IMP:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0055062; P:phosphate ion homeostasis; IMP:TAIR.
DR GO; GO:0051174; P:regulation of phosphorus metabolic process; IMP:TAIR.
DR CDD; cd00839; MPP_PAPs; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041792; MPP_PAP.
DR InterPro; IPR039331; PPA-like.
DR InterPro; IPR008963; Purple_acid_Pase-like_N.
DR InterPro; IPR015914; Purple_acid_Pase_N.
DR InterPro; IPR025733; Purple_acid_PPase_C_dom.
DR PANTHER; PTHR22953; PTHR22953; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF14008; Metallophos_C; 1.
DR Pfam; PF16656; Pur_ac_phosph_N; 1.
DR SUPFAM; SSF49363; SSF49363; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Hydrogen peroxide; Hydrolase;
KW Iron; Metal-binding; Oxidoreductase; Peroxidase; Reference proteome;
KW Signal; Vacuole; Zinc.
FT SIGNAL 1..30
FT /evidence="ECO:0000269|PubMed:16963519"
FT CHAIN 31..475
FT /note="Bifunctional purple acid phosphatase 26"
FT /id="PRO_0000333285"
FT ACT_SITE 322
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 349..351
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 349
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 351
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:16963519"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:16963519"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:16963519"
FT CONFLICT 46
FT /note="K -> N (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="R -> G (in Ref. 1; AAW29950)"
FT /evidence="ECO:0000305"
FT CONFLICT 419
FT /note="D -> G (in Ref. 1; AAW29950)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 475 AA; 55010 MW; 7C73A161EE16327E CRC64;
MNHLVIISVF LSSVLLLYRG ESGITSSFIR SEWPAVDIPL DHHVFKVPKG YNAPQQVHIT
QGDYDGKAVI ISWVTPDEPG SSQVHYGAVQ GKYEFVAQGT YHNYTFYKYK SGFIHHCLVS
DLEHDTKYYY KIESGESSRE FWFVTPPHVH PDASYKFGII GDMGQTFNSL STLEHYMESG
AQAVLFLGDL SYADRYQYND VGVRWDSWGR FVERSTAYQP WLWSAGNHEV DYMPYMGEVT
PFRNYLQRYT TPYLASKSSS PLWYAVRRAS AHIIVLSSYS PFVKYTPQWH WLSEELTRVD
REKTPWLIVL MHVPIYNSNE AHFMEGESMR AAFEEWFVQH KVDVIFAGHV HAYERSYRIS
NVRYNVSSGD RYPVPDKSAP VYITVGDGGN QEGLAGRFTE PQPDYSAFRE ASYGHSTLDI
KNRTHAIYHW NRNDDGKKVA TDEFVLHNQY WGKNIRRRKL KKHYIRSVVG GWIAT
