Bifunctional purple acid phosphatase 26 precursor - Arabidopsis thaliana (Mouse-ear cress)

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Q949Y3 (PPA26_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 79. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

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

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › 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 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: K_M=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 Reference proteome
Gene Ontology (GO)
Biological_process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW phosphate ion homeostasis Inferred from mutant phenotype PubMed 20348213. Source: TAIR
Cellular_component	cytosol Inferred from direct assay PubMed 21166475. Source: TAIR plant-type cell wall Inferred from direct assay PubMed 17526915. Source: TAIR vacuole Inferred from direct assay Ref.8 Ref.7 PubMed 20348213. Source: TAIR
Molecular_function	acid phosphatase activity Inferred from mutant phenotype PubMed 23125358. Source: TAIR metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW peroxidase activity 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

Ref.5

Chain

31 – 475

445

Bifunctional purple acid phosphatase 26

PRO_0000333285

Regions

Region

349 – 351

Substrate binding By similarity

Sites

Active site

322

Proton donor By similarity

Metal binding

162

Iron By similarity

Metal binding

189

Iron By similarity

Metal binding

189

Zinc By similarity

Metal binding

192

Iron By similarity

Metal binding

227

Zinc By similarity

Metal binding

312

Zinc By similarity

Metal binding

349

Zinc By similarity

Metal binding

351

Iron By similarity

Binding site

227

Substrate By similarity

Amino acid modifications

Glycosylation

103

N-linked (GlcNAc...) Probable

Glycosylation

365

N-linked (GlcNAc...) Probable

Glycosylation

422

N-linked (GlcNAc...) Probable

Experimental info

Sequence conflict

K → N AA sequence Ref.5

Sequence conflict

301

R → G in AAW29950. Ref.1

Sequence conflict

419

D → G in AAW29950. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q949Y3 [UniParc].

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

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

« Hide

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] [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. 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. 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.
IPI	IPI00539302.
RefSeq	NP_198334.1. NM_122874.3.
UniGene	At.20088.
3D structure databases
HSSP	HSSP built from PDB template 4KBP based on UniProtKB P80366.
ProteinModelPortal	Q949Y3.
SMR	Q949Y3. Positions 36-452.
ModBase	Search...
Proteomic databases
PaxDb	Q949Y3.
PRIDE	Q949Y3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G34850.1; AT5G34850.1; AT5G34850.
GeneID	833406.
KEGG	ath:AT5G34850.
Organism-specific databases
TAIR	At5g34850.
Phylogenomic databases
eggNOG	COG1409.
HOGENOM	HOG000238330.
InParanoid	Q949Y3.
OMA	NRTHAIY.
PhylomeDB	Q949Y3.
ProtClustDB	CLSN2687578.
Gene expression databases
Genevestigator	Q949Y3.
Family and domain databases
Gene3D	2.60.40.380. 1 hit.
InterPro	IPR004843. Metallo_PEstase_dom. IPR008963. Purple_acid_Pase-like_N. IPR015914. Purple_acid_Pase_N. IPR025733. Purple_acid_PPase_C_dom. [Graphical view]
Pfam	PF00149. Metallophos. 1 hit. PF14008. Metallophos_C. 1 hit. [Graphical view]
SUPFAM	SSF49363. Purple_Pase_N. 1 hit.
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:	May 1, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Including the following 2 domains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents