Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9SDZ9 (PPAF2_IPOBA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 2

EC=3.1.3.2
Alternative name(s):
Manganese(II) purple acid phosphatase 2
Gene names
Name:PAP2
OrganismIpomoea batatas (Sweet potato) (Convolvulus batatas)
Taxonomic identifier4120 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesConvolvulaceaeIpomoeeaeIpomoea

Protein attributes

Sequence length465 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

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

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

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)

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandIron
Metal-binding
Zinc
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
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 – 3232 Potential
Chain33 – 465433Purple acid phosphatase 2
PRO_5000057352

Regions

Region352 – 3543Substrate binding By similarity

Sites

Active site3251Proton donor By similarity
Metal binding1641Iron By similarity
Metal binding1931Iron By similarity
Metal binding1931Manganese By similarity
Metal binding1961Iron By similarity
Metal binding2301Manganese By similarity
Metal binding3151Manganese By similarity
Metal binding3521Manganese By similarity
Metal binding3541Iron By similarity
Binding site2301Substrate By similarity

Amino acid modifications

Glycosylation1101N-linked (GlcNAc...) Potential
Glycosylation1381N-linked (GlcNAc...) Potential
Glycosylation1721N-linked (GlcNAc...) Potential
Glycosylation3031N-linked (GlcNAc...) Potential
Glycosylation4001N-linked (GlcNAc...) Potential
Glycosylation4251N-linked (GlcNAc...) Potential
Disulfide bond374Interchain By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9SDZ9 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 49C0DCBA1CD8DF72

FASTA46553,401
        10         20         30         40         50         60 
MGASRTGCYL LAVVLAAVMN AAIAGITSSF IRKVEKTVDM PLDSDVFRVP PGYNAPQQVH 

        70         80         90        100        110        120 
ITQGDHVGKA MIVSWVTVDE PGSSKVVYWS ENSQHKKVAR GNIRTYTYFN YTSGYIHHCT 

       130        140        150        160        170        180 
IRNLEYNTKY YYEVGIGNTT RSFWFTTPPE VGPDVPYTFG LIGDLGQSFD SNRTLTHYER 

       190        200        210        220        230        240 
NPIKGQAVLF VGDLSYADNY PNHDNVRWDT WGRFVERSTA YQPWIWTAGN HEIDFAPEIG 

       250        260        270        280        290        300 
ETKPFKPFTK RYHVPYKASG STETFWYPIK RASAYIIVLS SYSAYGKYTP QYKWLEEELP 

       310        320        330        340        350        360 
KVNRTETPWL IVLMHSPWYN SYNYHYMEGE TMRVMYEPWF VQHKVDLVFA GHVHAYERSE 

       370        380        390        400        410        420 
RVSNVAYDIV NGKCTPVRDQ SAPVYITIGD GGNLEGLATN MTDPQPEYSA FREASFGHAT 

       430        440        450        460 
LDIKNRTHAY YSWHRNQDGY AVEADSMWVS NRFWHPVDDS TTTKL 

« 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF200826 mRNA. Translation: AAF19822.1.
PIRT51095.

3D structure databases

ProteinModelPortalQ9SDZ9.
SMRQ9SDZ9. Positions 39-461.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-15154.

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...

Entry information

Entry namePPAF2_IPOBA
AccessionPrimary (citable) accession number: Q9SDZ9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: May 1, 2000
Last modified: June 11, 2014
This is version 55 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