Reviewed, UniProtKB/Swiss-Prot P80366 (PPAF_PHAVU)

Names and origin

Protein names	Recommended name:     Fe(3+)-Zn(2+) purple acid phosphatase       Short name=PAP     EC=3.1.3.2 Alternative name(s):     Iron(III)-zinc(II) purple acid phosphatase
Organism	Phaseolus vulgaris (Kidney bean) (French bean)
Taxonomic identifier	3885 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Fabales › Fabaceae › Papilionoideae › Phaseoleae › Phaseolus

Protein attributes

Sequence length	432 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	A phosphate monoester + H2O = an alcohol + phosphate.
Cofactor	Binds 1 iron ion per subunit. Binds 1 zinc ion per subunit.
Subunit structure	Homodimer; disulfide-linked.
Subcellular location	Secreted.
Post-translational modification	The C-terminus of the enzyme is often modified by the removal of four terminal residues.
Sequence similarities	Belongs to the metallophosphoesterase superfamily. Purple acid phosphatase family.

Ontologies

Keywords
Cellular component	Secreted
Ligand	Iron Metal-binding Zinc
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Direct protein sequencing
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

Chain

1 – 432

432

Fe(3+)-Zn(2+) purple acid phosphatase

PRO_0000114474

Sites

Active site

296

1

Proton donor

Metal binding

135

1

Iron

Metal binding

164

1

Iron

Metal binding

164

1

Zinc

Metal binding

167

1

Iron

Metal binding

201

1

Zinc

Metal binding

286

1

Zinc

Metal binding

323

1

Zinc

Metal binding

325

1

Iron

Amino acid modifications

Glycosylation

81

1

N-linked (GlcNAc...); partial

Glycosylation

109

1

N-linked (GlcNAc...)

Glycosylation

143

1

N-linked (GlcNAc...)

Glycosylation

211

1

N-linked (GlcNAc...)

Glycosylation

396

1

N-linked (GlcNAc...)

Disulfide bond

345

Interchain

Secondary structure

1

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432

Helix Strand Turn

Details...

Helix

16 – 18

3

Beta strand

28 – 34

7

Beta strand

36 – 51

16

Beta strand

56 – 64

9

Beta strand

68 – 71

4

Beta strand

73 – 75

3

Beta strand

86 – 94

9

Beta strand

100 – 105

6

Beta strand

108 – 110

3

Beta strand

112 – 117

6

Beta strand

128 – 133

6

Helix

140 – 151

12

Beta strand

158 – 161

4

Helix

168 – 170

3

Helix

172 – 174

3

Helix

177 – 185

9

Helix

187 – 190

4

Beta strand

195 – 197

3

Helix

201 – 203

3

Helix

208 – 210

3

Helix

217 – 222

6

Turn

227 – 231

5

Beta strand

237 – 242

6

Beta strand

245 – 249

5

Helix

261 – 270

10

Turn

275 – 277

3

Beta strand

280 – 284

5

Turn

295 – 300

6

Helix

301 – 313

13

Beta strand

318 – 321

4

Beta strand

323 – 330

8

Beta strand

332 – 334

3

Beta strand

340 – 342

3

Beta strand

355 – 359

5

Turn

364 – 366

3

Beta strand

380 – 384

5

Beta strand

388 – 394

7

Beta strand

396 – 406

11

Beta strand

414 – 421

8

Turn

423 – 425

3

Sequences

	Sequence		Length	Mass (Da)
	P80366-1 [UniParc]. Last modified November 1, 1995. Version 2. Checksum: D2A60BCD9385A886	FASTA	432	50,236
	10 20 30 40 50 60 FVRKTNKNRD MPLDSDVFRV PPGYNAPQQV HITQGDLVGR AMIISWVTMD EPGSSAVRYW 70 80 90 100 110 120 SEKNGRKRIA KGKMSTYRFF NYSSGFIHHT TIRKLKYNTK YYYEVGLRNT TRRFSFITPP 130 140 150 160 170 180 QTGLDVPYTF GLIGDLGQSF DSNTTLSHYE LSPKKGQTVL FVGDLSYADR YPNHDNVRWD 190 200 210 220 230 240 TWGRFTERSV AYQPWIWTAG NHEIEFAPEI NETEPFKPFS YRYHVPYEAS QSTSPFWYSI 250 260 270 280 290 300 KRASAHIIVL SSHIAYGRGT PQYTWLKKEL RKVKRSETPW LIVLMHSPLY NSYNHHFMEG 310 320 330 340 350 360 EAMRTKFEAW FVKYKVDVVF AGHVHAYERS ERVSNIAYKI TDGLCTPVKD QSAPVYITIG 370 380 390 400 410 420 DAGNYGVIDS NMIQPQPEYS AFREASFGHG MFDIKNRTHA HFSWNRNQDG VAVEADSVWF 430 FNRHWYPVDD ST

References

[1]	"The amino acid sequence of the red kidney bean Fe(III)-Zn(II) purple acid phosphatase. Determination of the amino acid sequence by a combination of matrix-assisted laser desorption/ionization mass spectrometry and automated Edman sequencing." Klabunde T., Stahl B., Suerbaum H., Hahner S., Karas M., Hillenkamp F., Krebs B., Witzel H. Eur. J. Biochem. 226:369-375(1994) [PubMed: 8001554] [Abstract] Cited for: PROTEIN SEQUENCE.
[2]	"The oligosaccharides of the Fe(III)-Zn(II) purple acid phosphatase of the red kidney bean. Determination of the structure by a combination of matrix-assisted laser desorption/ionization mass spectrometry and selective enzymic degradation." Stahl B., Klabunde T., Witzel H., Krebs B., Steup M., Karas M., Hillenkamp F. Eur. J. Biochem. 220:321-330(1994) [PubMed: 8125089] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, STRUCTURE OF CARBOHYDRATES. Tissue: Seed.
[3]	"Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on crystal structures." Klabunde T., Straeter N., Froehlich R., Witzel H., Krebs B. J. Mol. Biol. 259:737-748(1996) [PubMed: 8683579] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).
[4]	"Crystal structure of a purple acid phosphatase containing a dinuclear Fe(III)-Zn(II) active site." Straeter N., Klabunde T., Tucker P., Witzel H., Krebs B. Science 268:1489-1492(1995) [PubMed: 7770774] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KBP	X-ray	2.65	A/B/C/D	1-432	[»]
2QFP	X-ray	2.20	A/B/C/D	9-432	[»]
2QFR	X-ray	2.40	A/B	9-432	[»]
3KBP	X-ray	3.00	A/B/C/D	1-432	[»]
4KBP	X-ray	2.70	A/B/C/D	1-432	[»]

ModBase

Search...

PTM databases

GlycoSuiteDB

P80366.

Enzyme and pathway databases

BRENDA

3.1.3.2. 8.

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

PPAF_PHAVU

Accession

Primary (citable) accession number: P80366

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	November 1, 1995
Last modified:	June 16, 2009
This is version 67 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)