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Q949Y3 (PPA26_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional purple acid phosphatase 26

Including the following 2 domains:

  1. Acid phosphatase
    EC=3.1.3.2
  2. Peroxidase
    EC=1.11.1.7
Gene names
Name:PAP26
Ordered Locus Names:At5g34850
ORF Names:T5E15.10
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length475 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5

Catalytic activity

A phosphate monoester + H2O = an alcohol + phosphate.

2 phenolic donor + H2O2 = 2 phenoxyl radical of the donor + 2 H2O.

Cofactor

Binds 1 iron ion per subunit By similarity.

Binds 1 zinc ion per subunit By similarity.

Enzyme regulation

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.

Subunit structure

Homodimer.

Subcellular location

Vacuole Ref.5 Ref.7 Ref.8.

Tissue specificity

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

Induction

Not induced at the transcription level by phosphate starvation, but accumulation of the protein in starved shoots. Ref.5

Post-translational modification

Glycosylated. Ref.5

Sequence similarities

Belongs to the metallophosphoesterase superfamily. Purple acid phosphatase family.

Biophysicochemical properties

Absorption:

Abs(max)=520 nm Ref.5

Kinetic parameters:

KM=0.8 mM for phosphoenolpyruvate (for the phosphatase activity)

pH dependence:

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Ref.5
Chain31 – 475445Bifunctional purple acid phosphatase 26
PRO_0000333285

Regions

Region349 – 3513Substrate binding By similarity

Sites

Active site3221Proton donor By similarity
Metal binding1621Iron By similarity
Metal binding1891Iron By similarity
Metal binding1891Zinc By similarity
Metal binding1921Iron By similarity
Metal binding2271Zinc By similarity
Metal binding3121Zinc By similarity
Metal binding3491Zinc By similarity
Metal binding3511Iron By similarity
Binding site2271Substrate By similarity

Amino acid modifications

Glycosylation1031N-linked (GlcNAc...) Probable
Glycosylation3651N-linked (GlcNAc...) Probable
Glycosylation4221N-linked (GlcNAc...) Probable

Experimental info

Sequence conflict461K → N AA sequence Ref.5
Sequence conflict3011R → G in AAW29950. Ref.1
Sequence conflict4191D → G in AAW29950. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q949Y3 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 7C73A161EE16327E

FASTA47555,010
        10         20         30         40         50         60 
MNHLVIISVF LSSVLLLYRG ESGITSSFIR SEWPAVDIPL DHHVFKVPKG YNAPQQVHIT 

        70         80         90        100        110        120 
QGDYDGKAVI ISWVTPDEPG SSQVHYGAVQ GKYEFVAQGT YHNYTFYKYK SGFIHHCLVS 

       130        140        150        160        170        180 
DLEHDTKYYY KIESGESSRE FWFVTPPHVH PDASYKFGII GDMGQTFNSL STLEHYMESG 

       190        200        210        220        230        240 
AQAVLFLGDL SYADRYQYND VGVRWDSWGR FVERSTAYQP WLWSAGNHEV DYMPYMGEVT 

       250        260        270        280        290        300 
PFRNYLQRYT TPYLASKSSS PLWYAVRRAS AHIIVLSSYS PFVKYTPQWH WLSEELTRVD 

       310        320        330        340        350        360 
REKTPWLIVL MHVPIYNSNE AHFMEGESMR AAFEEWFVQH KVDVIFAGHV HAYERSYRIS 

       370        380        390        400        410        420 
NVRYNVSSGD RYPVPDKSAP VYITVGDGGN QEGLAGRFTE PQPDYSAFRE ASYGHSTLDI 

       430        440        450        460        470 
KNRTHAIYHW NRNDDGKKVA TDEFVLHNQY WGKNIRRRKL KKHYIRSVVG GWIAT 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_198334.1. NM_122874.3.
UniGeneAt.20088.

3D structure databases

ProteinModelPortalQ949Y3.
SMRQ949Y3. Positions 36-452.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ949Y3.
PRIDEQ949Y3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G34850.1; AT5G34850.1; AT5G34850.
GeneID833406.
KEGGath:AT5G34850.

Organism-specific databases

TAIRAT5G34850.

Phylogenomic databases

eggNOGCOG1409.
HOGENOMHOG000238330.
InParanoidQ949Y3.
OMADQKAEGT.
PhylomeDBQ949Y3.

Gene expression databases

GenevestigatorQ949Y3.

Family and domain databases

Gene3D2.60.40.380. 1 hit.
3.60.21.10. 1 hit.
InterProIPR004843. 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]
PfamPF00149. Metallophos. 1 hit.
PF14008. Metallophos_C. 1 hit.
[Graphical view]
SUPFAMSSF49363. SSF49363. 1 hit.
SSF56300. SSF56300. 1 hit.
ProtoNetSearch...

Entry information

Entry namePPA26_ARATH
AccessionPrimary (citable) accession number: Q949Y3
Secondary accession number(s): Q5MAU9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: December 1, 2001
Last modified: June 11, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names