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Q9SE00 (PPAF1_IPOBA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Purple acid phosphatase 1

EC=3.1.3.2
Alternative name(s):
Manganese(II) purple acid phosphatase 1
Gene names
Name:PAP1
OrganismIpomoea batatas (Sweet potato) (Convolvulus batatas)
Taxonomic identifier4120 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesConvolvulaceaeIpomoeeaeIpomoea

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

A phosphate monoester + H2O = an alcohol + phosphate. Ref.1

Cofactor

Binds 1 iron ion per subunit By similarity. Ref.1 Ref.2

Binds 1 manganese ion per subunit. Can also use zinc, copper and magnesium ions. Ref.1 Ref.2

Subunit structure

Homodimer; disulfide-linked By similarity.

Subcellular location

Secreted By similarity.

Sequence similarities

Belongs to the metallophosphoesterase superfamily. Purple acid phosphatase family.

Biophysicochemical properties

Absorption:

Abs(max)=560 nm Ref.1 Ref.2

Kinetic parameters:

KM=95 µM for p-NPP (at pH 4.9 and 25 degrees Celsius)

KM=120 µM for ATP (at pH 4.9 and 25 degrees Celsius)

KM=180 µM for ADP (at pH 4.9 and 25 degrees Celsius)

KM=360 µM for AMP (at pH 4.9 and 25 degrees Celsius)

KM=75 µM for pyrophosphate (at pH 4.9 and 25 degrees Celsius)

KM=490 µM for beta-glycerophosphate (at pH 4.9 and 25 degrees Celsius)

KM=44 µM for 4-nitrophenol phosphate (at pH 3.5)

KM=68 µM for 4-nitrophenol phosphate (at pH 4)

KM=68 µM for 4-nitrophenol phosphate (at pH 4.5)

KM=93 µM for 4-nitrophenol phosphate (at pH 5)

KM=330 µM for 4-nitrophenol phosphate (at pH 6)

KM=930 µM for 4-nitrophenol phosphate (at pH 6.5)

KM=1800 µM for 4-nitrophenol phosphate (at pH 7)

KM=5000 µM for 4-nitrophenol phosphate (at pH 8)

pH dependence:

Optimum pH is 4.5.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandIron
Metal-binding
Zinc
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionacid phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-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

Signal peptide1 – 3838 Potential
Chain39 – 473435Purple acid phosphatase 1
PRO_5000057351

Regions

Region360 – 3623Substrate binding By similarity

Sites

Active site3331Proton donor By similarity
Metal binding1721Iron By similarity
Metal binding2011Iron By similarity
Metal binding2011Manganese
Metal binding2041Iron By similarity
Metal binding2381Manganese
Metal binding3231Manganese
Metal binding3601Manganese
Metal binding3621Iron By similarity
Binding site2381Substrate By similarity

Amino acid modifications

Glycosylation1181N-linked (GlcNAc...) Potential
Glycosylation1801N-linked (GlcNAc...) Potential
Glycosylation3111N-linked (GlcNAc...) Potential
Glycosylation4331N-linked (GlcNAc...) Potential
Disulfide bond382Interchain By similarity

Secondary structure

........................................................................... 473
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9SE00 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: BAE4B807DADD95A7

FASTA47353,815
        10         20         30         40         50         60 
MRLVVVGLWC LILGLILNPT KFCDAGVTSS YVRKSLSALP NAEDVDMPWD SDVFAVPSGY 

        70         80         90        100        110        120 
NAPQQVHITQ GDYEGRGVII SWTTPYDKAG ANKVVYWSEN SKSQKRAMGT VVTYKYYNYT 

       130        140        150        160        170        180 
SAFIHHCTIK DLEYDTKYYY RLGFGDAKRQ FWFVTPPKPG PDVPYVFGLI GDIGQTHDSN 

       190        200        210        220        230        240 
TTLTHYEQNS AKGQAVLFMG DLSYSNRWPN HDNNRWDTWG RFSERSVAYQ PWIWTAGNHE 

       250        260        270        280        290        300 
IDYAPDIGEY QPFVPFTNRY PTPHEASGSG DPLWYAIKRA SAHIIVLSSY SGFVKYSPQY 

       310        320        330        340        350        360 
KWFTSELEKV NRSETPWLIV LVHAPLYNSY EAHYMEGEAM RAIFEPYFVY YKVDIVFSGH 

       370        380        390        400        410        420 
VHSYERSERV SNVAYNIVNA KCTPVSDESA PVYITIGDGG NSEGLASEMT QPQPSYSAFR 

       430        440        450        460        470 
EASFGHGIFD IKNRTHAHFS WHRNQDGASV EADSLWLLNR YWASEDASSM SAM 

« Hide

References

[1]"Binuclear metal centers in plant purple acid phosphatases: Fe-Mn in sweet potato and Fe-Zn in soybean."
Schenk G., Ge Y., Carrington L.E., Wynne C.J., Searle I.R., Carroll B.J., Hamilton S., de Jersey J.
Arch. Biochem. Biophys. 370:183-189(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: cv. Golden.
[2]"Phosphate forms an unusual tripodal complex with the Fe-Mn center of sweet potato purple acid phosphatase."
Schenk G., Gahan L.R., Carrington L.E., Mitic N., Valizadeh M., Hamilton S.E., de Jersey J., Guddat L.W.
Proc. Natl. Acad. Sci. U.S.A. 102:273-278(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 39-464 IN COMPLEX WITH SUBSTRATE AND COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF200825 mRNA. Translation: AAF19821.1.
PIRA59200.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XZWX-ray2.50A/B39-464[»]
ProteinModelPortalQ9SE00.
SMRQ9SE00. Positions 39-464.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-15153.

Family and domain databases

Gene3D2.60.40.380. 1 hit.
3.60.21.10. 1 hit.
InterProIPR004843. 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]
PfamPF00149. Metallophos. 1 hit.
PF14008. Metallophos_C. 1 hit.
[Graphical view]
SUPFAMSSF49363. SSF49363. 1 hit.
SSF56300. SSF56300. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9SE00.

Entry information

Entry namePPAF1_IPOBA
AccessionPrimary (citable) accession number: Q9SE00
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: May 1, 2000
Last modified: June 11, 2014
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references