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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: 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)DescriptionActionsGraphical viewLength
Metal bindingi162Iron2 Publications1
Metal bindingi191Iron2 Publications1
Metal bindingi191Zinc2 Publications1
Metal bindingi194Iron2 Publications1
Metal bindingi228Zinc2 Publications1
Metal bindingi313Zinc2 Publications1
Active sitei323Proton donor2 Publications1
Metal bindingi350Zinc2 Publications1
Metal bindingi352Iron2 Publications1

GO - Molecular functioni

  • acid phosphatase activity Source: UniProtKB
  • ferric iron binding Source: UniProtKB
  • zinc ion binding Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Iron, Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.1.3.2. 4746.

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL5670.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 221 PublicationSequence analysisAdd BLAST22
ChainiPRO_000011447423 – 459Fe(3+)-Zn(2+) purple acid phosphatase1 PublicationSequence analysisAdd BLAST437

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei23Blocked amino end (Gly)1 Publication1
Glycosylationi108N-linked (GlcNAc...); partial3 Publications1
Glycosylationi136N-linked (GlcNAc...)3 Publications1
Glycosylationi170N-linked (GlcNAc...)3 Publications1
Glycosylationi238N-linked (GlcNAc...)2 Publications1
Disulfide bondi372Interchain2 Publications
Glycosylationi423N-linked (GlcNAc...)3 Publications1

Keywords - PTMi

Disulfide bond, Glycoprotein

PTM databases

UniCarbKBiP80366.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.3 Publications

Chemistry databases

BindingDBiP80366.

Structurei

Secondary structure

1459
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi43 – 45Combined sources3
Beta strandi55 – 61Combined sources7
Beta strandi63 – 67Combined sources5
Beta strandi69 – 78Combined sources10
Beta strandi84 – 91Combined sources8
Beta strandi95 – 97Combined sources3
Beta strandi100 – 102Combined sources3
Beta strandi113 – 119Combined sources7
Beta strandi127 – 132Combined sources6
Beta strandi135 – 137Combined sources3
Beta strandi139 – 144Combined sources6
Beta strandi155 – 160Combined sources6
Helixi167 – 177Combined sources11
Beta strandi185 – 188Combined sources4
Helixi195 – 197Combined sources3
Helixi199 – 201Combined sources3
Helixi204 – 217Combined sources14
Beta strandi222 – 224Combined sources3
Helixi228 – 231Combined sources4
Helixi235 – 237Combined sources3
Helixi244 – 249Combined sources6
Helixi254 – 257Combined sources4
Beta strandi264 – 269Combined sources6
Beta strandi272 – 276Combined sources5
Helixi288 – 299Combined sources12
Turni302 – 304Combined sources3
Beta strandi307 – 311Combined sources5
Turni322 – 327Combined sources6
Helixi328 – 340Combined sources13
Beta strandi344 – 348Combined sources5
Beta strandi350 – 357Combined sources8
Beta strandi359 – 361Combined sources3
Beta strandi367 – 369Combined sources3
Beta strandi382 – 386Combined sources5
Turni391 – 393Combined sources3
Beta strandi407 – 411Combined sources5
Beta strandi415 – 421Combined sources7
Beta strandi423 – 433Combined sources11
Beta strandi442 – 448Combined sources7
Turni450 – 452Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KBPX-ray2.65A/B/C/D28-459[»]
2QFPX-ray2.20A/B/C/D36-459[»]
2QFRX-ray2.40A/B36-459[»]
3KBPX-ray3.00A/B/C/D28-459[»]
4DHLX-ray2.30A/B/C/D34-459[»]
4DSYX-ray2.30A/B/C/D34-459[»]
4DT2X-ray2.70A/B/C/D34-459[»]
4KBPX-ray2.70A/B/C/D28-459[»]
4KKZX-ray2.20A/B/C/D34-459[»]
ProteinModelPortaliP80366.
SMRiP80366.
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.
PF16656. Pur_ac_phosph_N. 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)DescriptionActionsGraphical viewLength
Sequence conflicti280 – 281YS → HI AA sequence (PubMed:8001554).2
Sequence conflicti369N → D AA sequence (PubMed:8001554).1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KBPX-ray2.65A/B/C/D28-459[»]
2QFPX-ray2.20A/B/C/D36-459[»]
2QFRX-ray2.40A/B36-459[»]
3KBPX-ray3.00A/B/C/D28-459[»]
4DHLX-ray2.30A/B/C/D34-459[»]
4DSYX-ray2.30A/B/C/D34-459[»]
4DT2X-ray2.70A/B/C/D34-459[»]
4KBPX-ray2.70A/B/C/D28-459[»]
4KKZX-ray2.20A/B/C/D34-459[»]
ProteinModelPortaliP80366.
SMRiP80366.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiP80366.
ChEMBLiCHEMBL5670.

PTM databases

UniCarbKBiP80366.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.1.3.2. 4746.

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.
PF16656. Pur_ac_phosph_N. 1 hit.
[Graphical view]
SUPFAMiSSF49363. SSF49363. 1 hit.
SSF56300. SSF56300. 1 hit.
ProtoNetiSearch...

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: November 30, 2016
This is version 105 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

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 one 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.