Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q949Y3

- PPA26_ARATH

UniProt

Q949Y3 - PPA26_ARATH

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Bifunctional purple acid phosphatase 26

Gene

PAP26

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - 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

Binds 1 iron ion per subunit.By similarity
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

  1. acid phosphatase activity Source: TAIR
  2. metal ion binding Source: UniProtKB-KW
  3. peroxidase activity Source: UniProtKB-KW

GO - Biological processi

  1. dephosphorylation Source: GOC
  2. hydrogen peroxide catabolic process Source: UniProtKB-KW
  3. 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

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: Chromosome 5

Organism-specific databases

TAIRiAT5G34850.

Subcellular locationi

Vacuole 3 Publications

GO - Cellular componenti

  1. cytosol Source: TAIR
  2. plant-type cell wall Source: TAIR
  3. 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

Gene expression databases

GenevestigatoriQ949Y3.

Interactioni

Subunit structurei

Homodimer.

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.
OMAiDQKAEGT.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
RefSeqi NP_198334.1. NM_122874.3.
UniGenei At.20088.

3D structure databases

ProteinModelPortali Q949Y3.
SMRi Q949Y3. Positions 36-452.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PaxDbi Q949Y3.
PRIDEi Q949Y3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT5G34850.1 ; AT5G34850.1 ; AT5G34850 .
GeneIDi 833406.
KEGGi ath:AT5G34850.

Organism-specific databases

TAIRi AT5G34850.

Phylogenomic databases

eggNOGi COG1409.
HOGENOMi HOG000238330.
InParanoidi Q949Y3.
OMAi DQKAEGT.
PhylomeDBi Q949Y3.

Gene expression databases

Genevestigatori Q949Y3.

Family and domain databases

Gene3Di 2.60.40.380. 1 hit.
3.60.21.10. 1 hit.
InterProi IPR004843. 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 ]
Pfami PF00149. Metallophos. 1 hit.
PF14008. Metallophos_C. 1 hit.
[Graphical view ]
SUPFAMi SSF49363. SSF49363. 1 hit.
SSF56300. SSF56300. 1 hit.
ProtoNeti Search...

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], IDENTIFICATION BY MASS SPECTROMETRY.

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: October 1, 2014
This is version 89 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