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P80366

- PPAF_PHAVU

UniProt

P80366 - PPAF_PHAVU

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
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 2 (01 Nov 1995)
      Previous versions | rss
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    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

    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-SubCell

    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

    FVRKTNKNRD MPLDSDVFRV PPGYNAPQQV HITQGDLVGR AMIISWVTMD    50
    EPGSSAVRYW SEKNGRKRIA KGKMSTYRFF NYSSGFIHHT TIRKLKYNTK 100
    YYYEVGLRNT TRRFSFITPP QTGLDVPYTF GLIGDLGQSF DSNTTLSHYE 150
    LSPKKGQTVL FVGDLSYADR YPNHDNVRWD TWGRFTERSV AYQPWIWTAG 200
    NHEIEFAPEI NETEPFKPFS YRYHVPYEAS QSTSPFWYSI KRASAHIIVL 250
    SSHIAYGRGT PQYTWLKKEL RKVKRSETPW LIVLMHSPLY NSYNHHFMEG 300
    EAMRTKFEAW FVKYKVDVVF AGHVHAYERS ERVSNIAYKI TDGLCTPVKD 350
    QSAPVYITIG DAGNYGVIDS NMIQPQPEYS AFREASFGHG MFDIKNRTHA 400
    HFSWNRNQDG VAVEADSVWF FNRHWYPVDD ST 432
    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 1, 2014
    This is version 92 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