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Protein

Bifunctional purple acid phosphatase 26

Gene

PAP26

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Metallo-phosphoesterase involved in phosphate metabolism. Acid phosphatase activity with phosphoenolpyruvate, inorganic pyrophosphate, phenyl-phosphate and p-nitrophenyl-phosphate as the most effective substrates. No activity with phytic acid, phosphocholine or bis-p-nitrophenyl-phosphate. Has a peroxidase activity at alkaline pH.1 Publication

Catalytic activityi

A phosphate monoester + H2O = an alcohol + phosphate.
2 phenolic donor + H2O2 = 2 phenoxyl radical of the donor + 2 H2O.

Cofactori

Protein has several cofactor binding sites:
  • Fe cationBy similarityNote: Binds 1 Fe cation per subunit.By similarity
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Enzyme regulationi

Activated by Mg2+, Co2+, Mn2+ and Ba2+. Inhibited by Fe2+, Cu2+, Zn2+, NaF, molybdate, arsenate, vanadate and inorganic phosphate. No effect of tartrate, Asp, Gln, glutathione, Asn, ascorbic acid and phosphite.

Absorptioni

Abs(max)=520 nm1 Publication

Kineticsi

  1. KM=0.8 mM for phosphoenolpyruvate (for the phosphatase activity)1 Publication

    pH dependencei

    Optimum pH is 5.6 for the phosphatase activity and 8.8 for the peroxidase activity.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi162 – 1621IronBy similarity
    Metal bindingi189 – 1891IronBy similarity
    Metal bindingi189 – 1891ZincBy similarity
    Metal bindingi192 – 1921IronBy similarity
    Metal bindingi227 – 2271ZincBy similarity
    Binding sitei227 – 2271SubstrateBy similarity
    Metal bindingi312 – 3121ZincBy similarity
    Active sitei322 – 3221Proton donorBy similarity
    Metal bindingi349 – 3491ZincBy similarity
    Metal bindingi351 – 3511IronBy similarity

    GO - Molecular functioni

    • acid phosphatase activity Source: TAIR
    • metal ion binding Source: UniProtKB-KW
    • peroxidase activity Source: UniProtKB-KW

    GO - Biological processi

    • dephosphorylation Source: GOC
    • hydrogen peroxide catabolic process Source: UniProtKB-KW
    • phosphate ion homeostasis Source: TAIR
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Oxidoreductase, Peroxidase

    Keywords - Biological processi

    Hydrogen peroxide

    Keywords - Ligandi

    Iron, Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi3.1.3.2. 399.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional purple acid phosphatase 26
    Including the following 2 domains:
    Acid phosphatase (EC:3.1.3.2)
    Peroxidase (EC:1.11.1.7)
    Gene namesi
    Name:PAP26
    Ordered Locus Names:At5g34850
    ORF Names:T5E15.10
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548 Componenti: Chromosome 5

    Organism-specific databases

    TAIRiAT5G34850.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: TAIR
    • plant-type cell wall Source: TAIR
    • vacuole Source: TAIR
    Complete GO annotation...

    Keywords - Cellular componenti

    Vacuole

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 30301 PublicationAdd
    BLAST
    Chaini31 – 475445Bifunctional purple acid phosphatase 26PRO_0000333285Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi103 – 1031N-linked (GlcNAc...)1 Publication
    Glycosylationi365 – 3651N-linked (GlcNAc...)1 Publication
    Glycosylationi422 – 4221N-linked (GlcNAc...)1 Publication

    Post-translational modificationi

    Glycosylated.1 Publication

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ949Y3.
    PRIDEiQ949Y3.

    Expressioni

    Tissue specificityi

    Expressed in roots, stems, leaves, flowers and siliques.1 Publication

    Inductioni

    Not induced at the transcription level by phosphate starvation, but accumulation of the protein in starved shoots.1 Publication

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    STRINGi3702.AT5G34850.1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ949Y3.
    SMRiQ949Y3. Positions 36-452.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni349 – 3513Substrate bindingBy similarity

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG1409.
    HOGENOMiHOG000238330.
    InParanoidiQ949Y3.
    OMAiSTLQHYE.
    PhylomeDBiQ949Y3.

    Family and domain databases

    Gene3Di2.60.40.380. 1 hit.
    3.60.21.10. 1 hit.
    InterProiIPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    IPR008963. Purple_acid_Pase-like_N.
    IPR015914. Purple_acid_Pase_N.
    IPR025733. Purple_acid_PPase_C_dom.
    [Graphical view]
    PfamiPF00149. Metallophos. 1 hit.
    PF14008. Metallophos_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF49363. SSF49363. 1 hit.
    SSF56300. SSF56300. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q949Y3-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MNHLVIISVF LSSVLLLYRG ESGITSSFIR SEWPAVDIPL DHHVFKVPKG
    60 70 80 90 100
    YNAPQQVHIT QGDYDGKAVI ISWVTPDEPG SSQVHYGAVQ GKYEFVAQGT
    110 120 130 140 150
    YHNYTFYKYK SGFIHHCLVS DLEHDTKYYY KIESGESSRE FWFVTPPHVH
    160 170 180 190 200
    PDASYKFGII GDMGQTFNSL STLEHYMESG AQAVLFLGDL SYADRYQYND
    210 220 230 240 250
    VGVRWDSWGR FVERSTAYQP WLWSAGNHEV DYMPYMGEVT PFRNYLQRYT
    260 270 280 290 300
    TPYLASKSSS PLWYAVRRAS AHIIVLSSYS PFVKYTPQWH WLSEELTRVD
    310 320 330 340 350
    REKTPWLIVL MHVPIYNSNE AHFMEGESMR AAFEEWFVQH KVDVIFAGHV
    360 370 380 390 400
    HAYERSYRIS NVRYNVSSGD RYPVPDKSAP VYITVGDGGN QEGLAGRFTE
    410 420 430 440 450
    PQPDYSAFRE ASYGHSTLDI KNRTHAIYHW NRNDDGKKVA TDEFVLHNQY
    460 470
    WGKNIRRRKL KKHYIRSVVG GWIAT
    Length:475
    Mass (Da):55,010
    Last modified:December 1, 2001 - v1
    Checksum:i7C73A161EE16327E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti46 – 461K → N AA sequence (PubMed:16963519).Curated
    Sequence conflicti301 – 3011R → G in AAW29950 (PubMed:16244908).Curated
    Sequence conflicti419 – 4191D → G in AAW29950 (PubMed:16244908).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY842026 mRNA. Translation: AAW29950.1.
    AC019013 Genomic DNA. No translation available.
    CP002688 Genomic DNA. Translation: AED93912.1.
    AY050812 mRNA. Translation: AAK92747.1.
    AY091415 mRNA. Translation: AAM14354.1.
    RefSeqiNP_198334.1. NM_122874.3.
    UniGeneiAt.20088.

    Genome annotation databases

    EnsemblPlantsiAT5G34850.1; AT5G34850.1; AT5G34850.
    GeneIDi833406.
    KEGGiath:AT5G34850.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY842026 mRNA. Translation: AAW29950.1.
    AC019013 Genomic DNA. No translation available.
    CP002688 Genomic DNA. Translation: AED93912.1.
    AY050812 mRNA. Translation: AAK92747.1.
    AY091415 mRNA. Translation: AAM14354.1.
    RefSeqiNP_198334.1. NM_122874.3.
    UniGeneiAt.20088.

    3D structure databases

    ProteinModelPortaliQ949Y3.
    SMRiQ949Y3. Positions 36-452.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi3702.AT5G34850.1.

    Proteomic databases

    PaxDbiQ949Y3.
    PRIDEiQ949Y3.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT5G34850.1; AT5G34850.1; AT5G34850.
    GeneIDi833406.
    KEGGiath:AT5G34850.

    Organism-specific databases

    TAIRiAT5G34850.

    Phylogenomic databases

    eggNOGiCOG1409.
    HOGENOMiHOG000238330.
    InParanoidiQ949Y3.
    OMAiSTLQHYE.
    PhylomeDBiQ949Y3.

    Enzyme and pathway databases

    BRENDAi3.1.3.2. 399.

    Miscellaneous databases

    PROiQ949Y3.

    Family and domain databases

    Gene3Di2.60.40.380. 1 hit.
    3.60.21.10. 1 hit.
    InterProiIPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    IPR008963. Purple_acid_Pase-like_N.
    IPR015914. Purple_acid_Pase_N.
    IPR025733. Purple_acid_PPase_C_dom.
    [Graphical view]
    PfamiPF00149. Metallophos. 1 hit.
    PF14008. Metallophos_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF49363. SSF49363. 1 hit.
    SSF56300. SSF56300. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Expression patterns of purple acid phosphatase genes in Arabidopsis organs and functional analysis of AtPAP23 predominantly transcribed in flower."
      Zhu H., Qian W., Lu X., Li D., Liu X., Liu K., Wang D.
      Plant Mol. Biol. 59:581-594(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Strain: cv. Columbia.
    2. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
      Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
      , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
      Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    5. "Biochemical and molecular characterization of AtPAP26, a vacuolar purple acid phosphatase up-regulated in phosphate-deprived Arabidopsis suspension cells and seedlings."
      Veljanovski V., Vanderbeld B., Knowles V.L., Snedden W.A., Plaxton W.C.
      Plant Physiol. 142:1282-1293(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 31-53, FUNCTION, GLYCOSYLATION, CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, SUBCELLULAR LOCATION.
    6. "Purple acid phosphatases of Arabidopsis thaliana. Comparative analysis and differential regulation by phosphate deprivation."
      Li D., Zhu H., Liu K., Liu X., Leggewie G., Udvardi M., Wang D.
      J. Biol. Chem. 277:27772-27781(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY, NOMENCLATURE.
    7. "The vegetative vacuole proteome of Arabidopsis thaliana reveals predicted and unexpected proteins."
      Carter C., Pan S., Zouhar J., Avila E.L., Girke T., Raikhel N.V.
      Plant Cell 16:3285-3303(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    8. "Isolation of intact vacuoles and proteomic analysis of tonoplast from suspension-cultured cells of Arabidopsis thaliana."
      Shimaoka T., Ohnishi M., Sazuka T., Mitsuhashi N., Hara-Nishimura I., Shimazaki K., Maeshima M., Yokota A., Tomizawa K., Mimura T.
      Plant Cell Physiol. 45:672-683(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPPA26_ARATH
    AccessioniPrimary (citable) accession number: Q949Y3
    Secondary accession number(s): Q5MAU9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: December 1, 2001
    Last modified: June 24, 2015
    This is version 95 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.