Reviewed, UniProtKB/Swiss-Prot Q949Y3 (PPA26_ARATH)

Names and origin

Protein names

Recommended name:
    Bifunctional purple acid phosphatase 26
Including the following 2 domains:
    1- Recommended name:
            Acid phosphatase
              EC=3.1.3.2
    2- Recommended name:
            Peroxidase
              EC=1.11.1.7

Gene names

Name:	PAP26
Ordered Locus Names:	At5g34850
ORF Names:	T5E15.10

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	475 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Metallo-phosphoesterase involved in phosphate metabolism. Acid phosphatase activity with posphoenolpyruvate, 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.4
Catalytic activity	A phosphate monoester + H2O = an alcohol + phosphate. Donor + H2O2 = oxidized 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.4 Ref.6 Ref.7.
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.4
Post-translational modification	Glycosylated. Ref.4
Sequence similarities	Belongs to the metallophosphoesterase superfamily. Purple acid phosphatase family.
Biophysicochemical properties	Absorption: Abs(max)=520 nm 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.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Vacuole
Domain	Signal
Ligand	Iron Metal-binding Zinc
Molecular function	Hydrolase Oxidoreductase Peroxidase
PTM	Glycoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	plant-type cell wall Inferred from direct assay. Source: TAIR vacuole Ref.6 Ref.7 Inferred from direct assay. Source: TAIR
Molecular function	acid phosphatase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW peroxidase activity Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 30	30	Ref.4
	Chain	31 – 475	445	Bifunctional purple acid phosphatase 26		PRO_0000333285
Regions
	Region	349 – 351	3	Substrate binding By similarity
Sites
	Active site	322	1	Proton donor By similarity
	Metal binding	162	1	Iron By similarity
	Metal binding	189	1	Iron By similarity
	Metal binding	189	1	Zinc By similarity
	Metal binding	192	1	Iron By similarity
	Metal binding	227	1	Zinc By similarity
	Metal binding	312	1	Zinc By similarity
	Metal binding	349	1	Zinc By similarity
	Metal binding	351	1	Iron By similarity
	Binding site	227	1	Substrate By similarity
Amino acid modifications
	Glycosylation	103	1	N-linked (GlcNAc...) Probable
	Glycosylation	365	1	N-linked (GlcNAc...) Probable
	Glycosylation	422	1	N-linked (GlcNAc...) Probable
Experimental info
	Sequence conflict	46	1	K → N AA sequence Ref.4
	Sequence conflict	301	1	R → G in AAW29950. Ref.1
	Sequence conflict	419	1	D → G in AAW29950. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q949Y3-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 7C73A161EE16327E	FASTA	475	55,010
	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

References

	« Hide 'large scale' referencesShow '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: 16244908] [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: 11130714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"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: 16963519] [Abstract] Cited for: PROTEIN SEQUENCE OF 31-53, FUNCTION, GLYCOSYLATION, CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, SUBCELLULAR LOCATION.
[5]	"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: 12021284] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.
[6]	"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: 15539469] [Abstract] Cited for: SUBCELLULAR LOCATION.
[7]	"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: 15215502] [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. AY050812 mRNA. Translation: AAK92747.1. AY091415 mRNA. Translation: AAM14354.1.
IPI	IPI00539302.
RefSeq	NP_198334.1.
UniGene	At.20088 Rsa.7404
3D structure databases
HSSP	HSSP built from PDB template 4KBP based on UniProtKB P80366.
SMR	Q949Y3. Positions 36-452.
ModBase	Search...
Proteomic databases
PRIDE	Q949Y3.
Genome annotation databases
GeneID	833406.
GenomeReviews	Gene locus AT5G34850 in contig BA000015_GR.
KEGG	ath:AT5G34850.
NMPDR	fig|3702.1.peg.25186.
Organism-specific databases
TAIR	At5g34850.
Phylogenomic databases
eggNOG	KOG1378.
HOGENOM	HBG316723.
InParanoid	Q949Y3.
OMA	PYLASKS.
PhylomeDB	Q949Y3.
Gene expression databases
Genevestigator	Q949Y3.
Family and domain databases
InterPro	IPR004843. M-pesterase. IPR008963. Purple_acid_Pase-like_N. IPR015914. Purple_acid_Pase_N. [Graphical view]
Gene3D	G3DSA:2.60.40.380. Purple_acid_Pase_N. 1 hit.
Pfam	PF00149. Metallophos. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PPA26_ARATH

Accession

Primary (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:	February 9, 2010
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)