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P80366

- PPAF_PHAVU

UniProt

P80366 - PPAF_PHAVU

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Protein

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

Gene
N/A
Organism
Phaseolus vulgaris (Kidney bean) (French bean)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

A phosphate monoester + H2O = an alcohol + phosphate.

Cofactori

Binds 1 iron ion per subunit.
Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi135 – 1351Iron
Metal bindingi164 – 1641Iron
Metal bindingi164 – 1641Zinc
Metal bindingi167 – 1671Iron
Metal bindingi201 – 2011Zinc
Metal bindingi286 – 2861Zinc
Active sitei296 – 2961Proton donor
Metal bindingi323 – 3231Zinc
Metal bindingi325 – 3251Iron

GO - Molecular functioni

  1. acid phosphatase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Iron, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Fe(3+)-Zn(2+) purple acid phosphatase (EC:3.1.3.2)
Short name:
PAP
Alternative name(s):
Iron(III)-zinc(II) purple acid phosphatase
OrganismiPhaseolus vulgaris (Kidney bean) (French bean)
Taxonomic identifieri3885 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaePhaseolus

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 432432Fe(3+)-Zn(2+) purple acid phosphatasePRO_0000114474Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi81 – 811N-linked (GlcNAc...); partial
Glycosylationi109 – 1091N-linked (GlcNAc...)
Glycosylationi143 – 1431N-linked (GlcNAc...)
Glycosylationi211 – 2111N-linked (GlcNAc...)
Disulfide bondi345 – 345Interchain
Glycosylationi396 – 3961N-linked (GlcNAc...)

Post-translational modificationi

The C-terminus of the enzyme is often modified by the removal of four terminal residues.

Keywords - PTMi

Disulfide bond, Glycoprotein

PTM databases

UniCarbKBiP80366.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.

Structurei

Secondary structure

1
432
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi16 – 183
Beta strandi28 – 347
Beta strandi36 – 405
Beta strandi42 – 5110
Beta strandi57 – 648
Beta strandi68 – 703
Beta strandi73 – 753
Beta strandi86 – 927
Beta strandi100 – 1056
Beta strandi108 – 1103
Beta strandi112 – 1176
Beta strandi128 – 1336
Helixi140 – 15011
Beta strandi158 – 1614
Helixi168 – 1703
Helixi172 – 1743
Helixi177 – 19014
Beta strandi195 – 1973
Helixi201 – 2044
Helixi208 – 2103
Helixi217 – 2226
Helixi227 – 2304
Beta strandi237 – 2426
Beta strandi245 – 2495
Helixi261 – 27212
Turni275 – 2773
Beta strandi280 – 2845
Turni295 – 3006
Helixi301 – 31313
Beta strandi317 – 3215
Beta strandi323 – 3308
Beta strandi332 – 3343
Beta strandi340 – 3423
Beta strandi355 – 3595
Turni364 – 3663
Beta strandi380 – 3845
Beta strandi388 – 3947
Beta strandi396 – 40611
Beta strandi415 – 4217
Turni423 – 4253

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
4KKZX-ray2.20A/B/C/D7-432[»]
ProteinModelPortaliP80366.
SMRiP80366. Positions 9-432.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80366.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di2.60.40.380. 1 hit.
3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR008963. Purple_acid_Pase-like_N.
IPR015914. Purple_acid_Pase_N.
IPR025733. Purple_acid_PPase_C_dom.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
PF14008. Metallophos_C. 1 hit.
[Graphical view]
SUPFAMiSSF49363. SSF49363. 1 hit.
SSF56300. SSF56300. 1 hit.

Sequencei

Sequence statusi: Complete.

P80366-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
FVRKTNKNRD MPLDSDVFRV PPGYNAPQQV HITQGDLVGR AMIISWVTMD
60 70 80 90 100
EPGSSAVRYW SEKNGRKRIA KGKMSTYRFF NYSSGFIHHT TIRKLKYNTK
110 120 130 140 150
YYYEVGLRNT TRRFSFITPP QTGLDVPYTF GLIGDLGQSF DSNTTLSHYE
160 170 180 190 200
LSPKKGQTVL FVGDLSYADR YPNHDNVRWD TWGRFTERSV AYQPWIWTAG
210 220 230 240 250
NHEIEFAPEI NETEPFKPFS YRYHVPYEAS QSTSPFWYSI KRASAHIIVL
260 270 280 290 300
SSHIAYGRGT PQYTWLKKEL RKVKRSETPW LIVLMHSPLY NSYNHHFMEG
310 320 330 340 350
EAMRTKFEAW FVKYKVDVVF AGHVHAYERS ERVSNIAYKI TDGLCTPVKD
360 370 380 390 400
QSAPVYITIG DAGNYGVIDS NMIQPQPEYS AFREASFGHG MFDIKNRTHA
410 420 430
HFSWNRNQDG VAVEADSVWF FNRHWYPVDD ST
Length:432
Mass (Da):50,236
Last modified:November 1, 1995 - v2
Checksum:iD2A60BCD9385A886
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
4KKZ X-ray 2.20 A/B/C/D 7-432 [» ]
ProteinModelPortali P80366.
SMRi P80366. Positions 9-432.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P80366.
ChEMBLi CHEMBL5670.

PTM databases

UniCarbKBi P80366.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P80366.

Family and domain databases

Gene3Di 2.60.40.380. 1 hit.
3.60.21.10. 1 hit.
InterProi IPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR008963. Purple_acid_Pase-like_N.
IPR015914. Purple_acid_Pase_N.
IPR025733. Purple_acid_PPase_C_dom.
[Graphical view ]
Pfami PF00149. Metallophos. 1 hit.
PF14008. Metallophos_C. 1 hit.
[Graphical view ]
SUPFAMi SSF49363. SSF49363. 1 hit.
SSF56300. SSF56300. 1 hit.
ProtoNeti Search...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).

Entry informationi

Entry nameiPPAF_PHAVU
AccessioniPrimary (citable) accession number: P80366
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 1, 1995
Last modified: October 29, 2014
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3