Reviewed, UniProtKB/Swiss-Prot Q9SE00 (PPAF1_IPOBA)

Names and origin

Protein names

Recommended name:
    Purple acid phosphatase 1
    EC=3.1.3.2
Alternative name(s):
    Manganese(II) purple acid phosphatase 1

Gene names

Name:

PAP1

Organism

Ipomoea batatas (Sweet potato) (Batate)

Taxonomic identifier

4120 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Convolvulaceae › Ipomoeeae › Ipomoea

Protein attributes

Sequence length	473 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)

Catalytic activity	A phosphate monoester + H2O = an alcohol + phosphate. Ref.1
Cofactor	Binds 1 iron ion per subunit By similarity. Binds 1 manganese ion per subunit. Can also use zinc, copper and magnesium ions. Ref.1 Ref.2
Subunit structure	Homodimer; disulfide-linked By similarity.
Subcellular location	Secreted By similarity.
Sequence similarities	Belongs to the metallophosphoesterase superfamily. Purple acid phosphatase family.
Biophysicochemical properties	Absorption: Abs(max)=560 nm Kinetic parameters: KM=95 µM for p-NPP (at pH 4.9 and 25 degrees Celsius) KM=120 µM for ATP (at pH 4.9 and 25 degrees Celsius) KM=180 µM for ADP (at pH 4.9 and 25 degrees Celsius) KM=360 µM for AMP (at pH 4.9 and 25 degrees Celsius) KM=75 µM for pyrophosphate (at pH 4.9 and 25 degrees Celsius) KM=490 µM for beta-glycerophosphate (at pH 4.9 and 25 degrees Celsius) KM=44 µM for 4-nitrophenol phosphate (at pH 3.5) KM=68 µM for 4-nitrophenol phosphate (at pH 4) KM=68 µM for 4-nitrophenol phosphate (at pH 4.5) KM=93 µM for 4-nitrophenol phosphate (at pH 5) KM=330 µM for 4-nitrophenol phosphate (at pH 6) KM=930 µM for 4-nitrophenol phosphate (at pH 6.5) KM=1800 µM for 4-nitrophenol phosphate (at pH 7) KM=5000 µM for 4-nitrophenol phosphate (at pH 8) pH dependence: Optimum pH is 4.5.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Iron Metal-binding Zinc
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure
Gene Ontology (GO)
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acid phosphatase activity Inferred from electronic annotation. Source: EC iron ion binding 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 – 38

38

Potential

Chain

39 – 473

435

Purple acid phosphatase 1

PRO_5000057351

Regions

Region

360 – 362

3

Substrate binding By similarity

Sites

Active site

333

1

Proton donor By similarity

Metal binding

172

1

Iron By similarity

Metal binding

201

1

Iron By similarity

Metal binding

201

1

Manganese

Metal binding

204

1

Iron By similarity

Metal binding

238

1

Manganese

Metal binding

323

1

Manganese

Metal binding

360

1

Manganese

Metal binding

362

1

Iron By similarity

Binding site

238

1

Substrate By similarity

Amino acid modifications

Glycosylation

118

1

N-linked (GlcNAc...) Potential

Glycosylation

180

1

N-linked (GlcNAc...) Potential

Glycosylation

311

1

N-linked (GlcNAc...) Potential

Glycosylation

433

1

N-linked (GlcNAc...) Potential

Disulfide bond

382

Interchain By similarity

Secondary structure

1

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473

Helix Strand Turn

Details...

Helix

42 – 45

4

Helix

52 – 54

3

Beta strand

64 – 69

6

Beta strand

79 – 86

8

Beta strand

94 – 98

5

Beta strand

105 – 107

3

Beta strand

123 – 128

6

Beta strand

137 – 142

6

Beta strand

149 – 154

6

Beta strand

165 – 167

3

Helix

177 – 188

12

Beta strand

196 – 198

3

Helix

205 – 207

3

Helix

209 – 211

3

Helix

214 – 218

5

Helix

224 – 227

4

Helix

254 – 259

6

Beta strand

274 – 279

6

Beta strand

282 – 286

5

Helix

298 – 309

12

Turn

312 – 314

3

Beta strand

317 – 321

5

Turn

332 – 335

4

Helix

339 – 350

12

Beta strand

354 – 358

5

Beta strand

362 – 367

6

Beta strand

369 – 371

3

Beta strand

392 – 395

4

Beta strand

417 – 421

5

Beta strand

429 – 431

3

Beta strand

434 – 441

8

Beta strand

452 – 458

7

Sequences

	Sequence		Length	Mass (Da)
	Q9SE00-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: BAE4B807DADD95A7	FASTA	473	53,815
	10 20 30 40 50 60 MRLVVVGLWC LILGLILNPT KFCDAGVTSS YVRKSLSALP NAEDVDMPWD SDVFAVPSGY 70 80 90 100 110 120 NAPQQVHITQ GDYEGRGVII SWTTPYDKAG ANKVVYWSEN SKSQKRAMGT VVTYKYYNYT 130 140 150 160 170 180 SAFIHHCTIK DLEYDTKYYY RLGFGDAKRQ FWFVTPPKPG PDVPYVFGLI GDIGQTHDSN 190 200 210 220 230 240 TTLTHYEQNS AKGQAVLFMG DLSYSNRWPN HDNNRWDTWG RFSERSVAYQ PWIWTAGNHE 250 260 270 280 290 300 IDYAPDIGEY QPFVPFTNRY PTPHEASGSG DPLWYAIKRA SAHIIVLSSY SGFVKYSPQY 310 320 330 340 350 360 KWFTSELEKV NRSETPWLIV LVHAPLYNSY EAHYMEGEAM RAIFEPYFVY YKVDIVFSGH 370 380 390 400 410 420 VHSYERSERV SNVAYNIVNA KCTPVSDESA PVYITIGDGG NSEGLASEMT QPQPSYSAFR 430 440 450 460 470 EASFGHGIFD IKNRTHAHFS WHRNQDGASV EADSLWLLNR YWASEDASSM SAM

References

[1]

"Binuclear metal centers in plant purple acid phosphatases: Fe-Mn in sweet potato and Fe-Zn in soybean." Schenk G., Ge Y., Carrington L.E., Wynne C.J., Searle I.R., Carroll B.J., Hamilton S., de Jersey J. Arch. Biochem. Biophys. 370:183-189(1999) [PubMed: 10510276] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES. Strain: cv. Golden.

[2]

"Phosphate forms an unusual tripodal complex with the Fe-Mn center of sweet potato purple acid phosphatase." Schenk G., Gahan L.R., Carrington L.E., Mitic N., Valizadeh M., Hamilton S.E., de Jersey J., Guddat L.W. Proc. Natl. Acad. Sci. U.S.A. 102:273-278(2005) [PubMed: 15625111] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 39-464 IN COMPLEX WITH SUBSTRATE AND COFACTORS, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF200825 mRNA. Translation: AAF19821.1.

PIR

A59200.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1XZW	X-ray	2.50	A/B	39-464	[»]

ModBase

Search...

Family and domain databases

InterPro

IPR004843. M-pesterase.
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

PPAF1_IPOBA

Accession

Primary (citable) accession number: Q9SE00

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	May 1, 2000
Last modified:	September 1, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)