Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

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

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

Functioni

Catalytic activityi

A phosphate monoester + H2O = an alcohol + phosphate.2 Publications

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Inhibited by compounds CC24201, CC27209, and MO07123 (PubMed:22943065). Inhibited by the tetraoxoanions molybdate and phosphate (PubMed:12054466). Not inhibited by EDTA or tartrate (PubMed:12054466).2 Publications

pH dependencei

Optimum pH is 6.1.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi162 – 1621Iron2 Publications
Metal bindingi191 – 1911Iron2 Publications
Metal bindingi191 – 1911Zinc2 Publications
Metal bindingi194 – 1941Iron2 Publications
Metal bindingi228 – 2281Zinc2 Publications
Metal bindingi313 – 3131Zinc2 Publications
Active sitei323 – 3231Proton donor2 Publications
Metal bindingi350 – 3501Zinc2 Publications
Metal bindingi352 – 3521Iron2 Publications

GO - Molecular functioni

  1. acid phosphatase activity Source: UniProtKB
  2. ferric iron binding Source: UniProtKB
  3. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. dephosphorylation Source: GOC
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 phosphatase1 Publication (EC:3.1.3.22 Publications)
Short name:
PAP1 Publication
Alternative name(s):
Iron(III)-zinc(II) purple acid phosphatase1 Publication
OrganismiPhaseolus vulgaris (Kidney bean) (French bean)
Taxonomic identifieri3885 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaePhaseolus

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 22221 PublicationSequence AnalysisAdd
BLAST
Chaini23 – 459437Fe(3+)-Zn(2+) purple acid phosphatase1 PublicationSequence AnalysisPRO_0000114474Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei23 – 231Blocked amino end (Gly)1 Publication
Glycosylationi108 – 1081N-linked (GlcNAc...); partial3 Publications
Glycosylationi136 – 1361N-linked (GlcNAc...)3 Publications
Glycosylationi170 – 1701N-linked (GlcNAc...)3 Publications
Glycosylationi238 – 2381N-linked (GlcNAc...)2 Publications
Disulfide bondi372 – 372Interchain2 Publications
Glycosylationi423 – 4231N-linked (GlcNAc...)3 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

PTM databases

UniCarbKBiP80366.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.3 Publications

Structurei

Secondary structure

1
459
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi16 – 183Combined sources
Beta strandi28 – 347Combined sources
Beta strandi36 – 405Combined sources
Beta strandi42 – 5110Combined sources
Beta strandi57 – 648Combined sources
Beta strandi68 – 703Combined sources
Beta strandi73 – 753Combined sources
Beta strandi86 – 927Combined sources
Beta strandi100 – 1056Combined sources
Beta strandi108 – 1103Combined sources
Beta strandi112 – 1176Combined sources
Beta strandi128 – 1336Combined sources
Helixi140 – 15011Combined sources
Beta strandi158 – 1614Combined sources
Helixi168 – 1703Combined sources
Helixi172 – 1743Combined sources
Helixi177 – 19014Combined sources
Beta strandi195 – 1973Combined sources
Helixi201 – 2044Combined sources
Helixi208 – 2103Combined sources
Helixi217 – 2226Combined sources
Helixi227 – 2304Combined sources
Beta strandi237 – 2426Combined sources
Beta strandi245 – 2495Combined sources
Helixi261 – 27212Combined sources
Turni275 – 2773Combined sources
Beta strandi280 – 2845Combined sources
Turni295 – 3006Combined sources
Helixi301 – 31313Combined sources
Beta strandi317 – 3215Combined sources
Beta strandi323 – 3308Combined sources
Beta strandi332 – 3343Combined sources
Beta strandi340 – 3423Combined sources
Beta strandi355 – 3595Combined sources
Turni364 – 3663Combined sources
Beta strandi380 – 3845Combined sources
Beta strandi388 – 3947Combined sources
Beta strandi396 – 40611Combined sources
Beta strandi415 – 4217Combined sources
Turni423 – 4253Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KBPX-ray2.65A/B/C/D36-459[»]
2QFPX-ray2.20A/B/C/D36-459[»]
2QFRX-ray2.40A/B36-459[»]
3KBPX-ray3.00A/B/C/D36-459[»]
4DHLX-ray2.30A/B/C/D35-458[»]
4DSYX-ray2.30A/B/C/D34-458[»]
4DT2X-ray2.70A/B/C/D34-459[»]
4KBPX-ray2.70A/B/C/D36-459[»]
4KKZX-ray2.20A/B/C/D35-458[»]
ProteinModelPortaliP80366.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80366.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P80366-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGVVKGLLAL ALVLNVVVVS NGGKSSNFVR KTNKNRDMPL DSDVFRVPPG
60 70 80 90 100
YNAPQQVHIT QGDLVGRAMI ISWVTMDEPG SSAVRYWSEK NGRKRIAKGK
110 120 130 140 150
MSTYRFFNYS SGFIHHTTIR KLKYNTKYYY EVGLRNTTRR FSFITPPQTG
160 170 180 190 200
LDVPYTFGLI GDLGQSFDSN TTLSHYELSP KKGQTVLFVG DLSYADRYPN
210 220 230 240 250
HDNVRWDTWG RFTERSVAYQ PWIWTAGNHE IEFAPEINET EPFKPFSYRY
260 270 280 290 300
HVPYEASQST SPFWYSIKRA SAHIIVLSSY SAYGRGTPQY TWLKKELRKV
310 320 330 340 350
KRSETPWLIV LMHSPLYNSY NHHFMEGEAM RTKFEAWFVK YKVDVVFAGH
360 370 380 390 400
VHAYERSERV SNIAYKITNG LCTPVKDQSA PVYITIGDAG NYGVIDSNMI
410 420 430 440 450
QPQPEYSAFR EASFGHGMFD IKNRTHAHFS WNRNQDGVAV EADSVWFFNR

HWYPVDDST
Length:459
Mass (Da):52,857
Last modified:November 26, 2014 - v3
Checksum:iCC379B7C1AE4D21A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti280 – 2812YS → HI AA sequence (PubMed:8001554)
Sequence conflicti369 – 3691N → D AA sequence (PubMed:8001554)

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001270 mRNA. Translation: CAA04644.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001270 mRNA. Translation: CAA04644.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KBPX-ray2.65A/B/C/D36-459[»]
2QFPX-ray2.20A/B/C/D36-459[»]
2QFRX-ray2.40A/B36-459[»]
3KBPX-ray3.00A/B/C/D36-459[»]
4DHLX-ray2.30A/B/C/D35-458[»]
4DSYX-ray2.30A/B/C/D34-458[»]
4DT2X-ray2.70A/B/C/D34-459[»]
4KBPX-ray2.70A/B/C/D36-459[»]
4KKZX-ray2.20A/B/C/D35-458[»]
ProteinModelPortaliP80366.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP80366.
ChEMBLiCHEMBL5670.

PTM databases

UniCarbKBiP80366.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP80366.

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.
ProtoNetiSearch...

Publicationsi

  1. "Heterologous expression and characterization of recombinant purple acid phosphatase from red kidney bean."
    Vogel A., Borchers T., Marcus K., Meyer H.E., Krebs B., Spener F.
    Arch. Biochem. Biophys. 401:164-172(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, BLOCKAGE OF N-TERMINUS.
    Tissue: SeedImported.
  2. "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 OF 28-459.
    Tissue: Seed1 Publication.
  3. "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, GLYCOSYLATION AT ASN-108; ASN-136; ASN-170; ASN-238 AND ASN-423.
    Tissue: Seed.
  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), COFACTOR, SUBUNIT, ACTIVE SITE.
  5. "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), COFACTOR, SUBUNIT, GLYCOSYLATION AT ASN-108; ASN-136; ASN-170; ASN-238 AND ASN-423, DISULFIDE BOND, ACTIVE SITE.
  6. "Identification of purple acid phosphatase inhibitors by fragment-based screening: promising new leads for osteoporosis therapeutics."
    Feder D., Hussein W.M., Clayton D.J., Kan M.W., Schenk G., McGeary R.P., Guddat L.W.
    Chem. Biol. Drug Des. 80:665-674(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 34-459 IN COMPLEX WITH INHIBITOR, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, SUBUNIT, DISULFIDE BOND, GLYCOSYLATION AT ASN-108; ASN-136; ASN-170 AND ASN-423.

Entry informationi

Entry nameiPPAF_PHAVU
AccessioniPrimary (citable) accession number: P80366
Secondary accession number(s): O24319
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 26, 2014
Last modified: February 4, 2015
This is version 96 of the entry and version 3 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.