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Protein

Purple acid phosphatase 2

Gene

PAP2

Organism
Ipomoea batatas (Sweet potato) (Convolvulus batatas)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:

Absorptioni

Abs(max)=560 nm1 Publication

Kineticsi

  1. KM=95 µM for p-NPP (at pH 4.9 and 25 degrees Celsius)1 Publication
  2. KM=120 µM for ATP (at pH 4.9 and 25 degrees Celsius)1 Publication
  3. KM=180 µM for ADP (at pH 4.9 and 25 degrees Celsius)1 Publication
  4. KM=360 µM for AMP (at pH 4.9 and 25 degrees Celsius)1 Publication
  5. KM=75 µM for pyrophosphate (at pH 4.9 and 25 degrees Celsius)1 Publication
  6. KM=490 µM for beta-glycerophosphate (at pH 4.9 and 25 degrees Celsius)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi164 – 1641IronBy similarity
    Metal bindingi193 – 1931IronBy similarity
    Metal bindingi193 – 1931ManganeseBy similarity
    Metal bindingi196 – 1961IronBy similarity
    Metal bindingi230 – 2301ManganeseBy similarity
    Binding sitei230 – 2301SubstrateBy similarity
    Metal bindingi315 – 3151ManganeseBy similarity
    Active sitei325 – 3251Proton donorBy similarity
    Metal bindingi352 – 3521ManganeseBy similarity
    Metal bindingi354 – 3541IronBy similarity

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Iron, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-15154.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Purple acid phosphatase 2 (EC:3.1.3.2)
    Alternative name(s):
    Manganese(II) purple acid phosphatase 2
    Gene namesi
    Name:PAP2
    OrganismiIpomoea batatas (Sweet potato) (Convolvulus batatas)
    Taxonomic identifieri4120 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesConvolvulaceaeIpomoeeaeIpomoea

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3232Sequence AnalysisAdd
    BLAST
    Chaini33 – 465433Purple acid phosphatase 2PRO_5000057352Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi110 – 1101N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi138 – 1381N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi172 – 1721N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi303 – 3031N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi374 – 374InterchainBy similarity
    Glycosylationi400 – 4001N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi425 – 4251N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ9SDZ9.
    SMRiQ9SDZ9. Positions 39-461.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni352 – 3543Substrate bindingBy similarity

    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.

    Q9SDZ9-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MGASRTGCYL LAVVLAAVMN AAIAGITSSF IRKVEKTVDM PLDSDVFRVP
    60 70 80 90 100
    PGYNAPQQVH ITQGDHVGKA MIVSWVTVDE PGSSKVVYWS ENSQHKKVAR
    110 120 130 140 150
    GNIRTYTYFN YTSGYIHHCT IRNLEYNTKY YYEVGIGNTT RSFWFTTPPE
    160 170 180 190 200
    VGPDVPYTFG LIGDLGQSFD SNRTLTHYER NPIKGQAVLF VGDLSYADNY
    210 220 230 240 250
    PNHDNVRWDT WGRFVERSTA YQPWIWTAGN HEIDFAPEIG ETKPFKPFTK
    260 270 280 290 300
    RYHVPYKASG STETFWYPIK RASAYIIVLS SYSAYGKYTP QYKWLEEELP
    310 320 330 340 350
    KVNRTETPWL IVLMHSPWYN SYNYHYMEGE TMRVMYEPWF VQHKVDLVFA
    360 370 380 390 400
    GHVHAYERSE RVSNVAYDIV NGKCTPVRDQ SAPVYITIGD GGNLEGLATN
    410 420 430 440 450
    MTDPQPEYSA FREASFGHAT LDIKNRTHAY YSWHRNQDGY AVEADSMWVS
    460
    NRFWHPVDDS TTTKL
    Length:465
    Mass (Da):53,401
    Last modified:May 1, 2000 - v1
    Checksum:i49C0DCBA1CD8DF72
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF200826 mRNA. Translation: AAF19822.1.
    PIRiT51095.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF200826 mRNA. Translation: AAF19822.1.
    PIRiT51095.

    3D structure databases

    ProteinModelPortaliQ9SDZ9.
    SMRiQ9SDZ9. Positions 39-461.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-15154.

    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. "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.

    Entry informationi

    Entry nameiPPAF2_IPOBA
    AccessioniPrimary (citable) accession number: Q9SDZ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 5, 2009
    Last sequence update: May 1, 2000
    Last modified: January 7, 2015
    This is version 59 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Documents

    1. 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.