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P80366 (PPAF_PHAVU) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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
OrganismPhaseolus vulgaris (Kidney bean) (French bean)
Taxonomic identifier3885 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Phaseoleae › Phaseolus

Protein attributes

Sequence length432 AA.
Sequence statusComplete.
Protein existenceEvidence 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 componentSecreted
   LigandIron
Metal-binding
Zinc
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionacid phosphatase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 432432Fe(3+)-Zn(2+) purple acid phosphatase
PRO_0000114474

Sites

Active site2961Proton donor
Metal binding1351Iron
Metal binding1641Iron
Metal binding1641Zinc
Metal binding1671Iron
Metal binding2011Zinc
Metal binding2861Zinc
Metal binding3231Zinc
Metal binding3251Iron

Amino acid modifications

Glycosylation811N-linked (GlcNAc...); partial
Glycosylation1091N-linked (GlcNAc...)
Glycosylation1431N-linked (GlcNAc...)
Glycosylation2111N-linked (GlcNAc...)
Glycosylation3961N-linked (GlcNAc...)
Disulfide bond345Interchain

Secondary structure

1 ................................................................................ 432
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P80366 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: D2A60BCD9385A886

FASTA43250,236
        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

« Hide

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

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KBPX-ray2.65A/B/C/D1-432[»]
2QFPX-ray2.20A/B/C/D9-432[»]
2QFRX-ray2.40A/B9-432[»]
3KBPX-ray3.00A/B/C/D1-432[»]
4KBPX-ray2.70A/B/C/D1-432[»]
ProteinModelPortalP80366.
SMRP80366. Positions 9-432.
ModBaseSearch...

PTM databases

GlycoSuiteDBP80366.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR004843. Metallo_PEstase_dom.
IPR008963. Purple_acid_Pase-like_N.
IPR015914. Purple_acid_Pase_N.
[Graphical view]
Gene3DG3DSA:2.60.40.380. Purple_acid_Pase_N. 1 hit.
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
SUPFAMSSF49363. Purple_Pase_N. 1 hit.
ProtoNetSearch...

Entry information

Entry namePPAF_PHAVU
AccessionPrimary (citable) accession number: P80366
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 1, 1995
Last modified: September 21, 2011
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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