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   27-MAR-2024, entry version 140.
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.Q949Y3; -.
DR   GlyCosmos; Q949Y3; 3 sites, No reported glycans.
DR   iPTMnet; Q949Y3; -.
DR   PaxDb; 3702-AT5G34850-1; -.
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; AT5G34850; PAP26.
DR   eggNOG; KOG1378; Eukaryota.
DR   HOGENOM; CLU_013387_0_1_1; -.
DR   InParanoid; Q949Y3; -.
DR   OMA; DMDSNDA; -.
DR   OrthoDB; 203742at2759; -.
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   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:0140825; F:lactoperoxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; 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   Gene3D; 2.60.40.380; Purple acid phosphatase-like, N-terminal; 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; ACID PHOSPHATASE RELATED; 1.
DR   PANTHER; PTHR22953:SF55; BIFUNCTIONAL PURPLE ACID PHOSPHATASE 26; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF14008; Metallophos_C; 1.
DR   Pfam; PF16656; Pur_ac_phosph_N; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   SUPFAM; SSF49363; Purple acid phosphatase, N-terminal domain; 1.
DR   Genevisible; Q949Y3; AT.
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
//