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Protein

Purple acid phosphatase 1

Gene

PAP1

Organism
Ipomoea batatas (Sweet potato) (Convolvulus batatas)
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.1 Publication

Cofactori

Protein has several cofactor binding sites:

Absorptioni

Abs(max)=560 nm2 Publications

Kineticsi

  1. KM=95 µM for p-NPP (at pH 4.9 and 25 degrees Celsius)2 Publications
  2. KM=120 µM for ATP (at pH 4.9 and 25 degrees Celsius)2 Publications
  3. KM=180 µM for ADP (at pH 4.9 and 25 degrees Celsius)2 Publications
  4. KM=360 µM for AMP (at pH 4.9 and 25 degrees Celsius)2 Publications
  5. KM=75 µM for pyrophosphate (at pH 4.9 and 25 degrees Celsius)2 Publications
  6. KM=490 µM for beta-glycerophosphate (at pH 4.9 and 25 degrees Celsius)2 Publications
  7. KM=44 µM for 4-nitrophenol phosphate (at pH 3.5)2 Publications
  8. KM=68 µM for 4-nitrophenol phosphate (at pH 4)2 Publications
  9. KM=68 µM for 4-nitrophenol phosphate (at pH 4.5)2 Publications
  10. KM=93 µM for 4-nitrophenol phosphate (at pH 5)2 Publications
  11. KM=330 µM for 4-nitrophenol phosphate (at pH 6)2 Publications
  12. KM=930 µM for 4-nitrophenol phosphate (at pH 6.5)2 Publications
  13. KM=1800 µM for 4-nitrophenol phosphate (at pH 7)2 Publications
  14. KM=5000 µM for 4-nitrophenol phosphate (at pH 8)2 Publications

    pH dependencei

    Optimum pH is 4.5.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi172 – 1721IronBy similarity
    Metal bindingi201 – 2011IronBy similarity
    Metal bindingi201 – 2011Manganese
    Metal bindingi204 – 2041IronBy similarity
    Metal bindingi238 – 2381Manganese
    Binding sitei238 – 2381SubstrateBy similarity
    Metal bindingi323 – 3231Manganese
    Active sitei333 – 3331Proton donorBy similarity
    Metal bindingi360 – 3601Manganese
    Metal bindingi362 – 3621IronBy similarity

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Iron, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-15153.
    BRENDAi3.1.3.2. 2773.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Purple acid phosphatase 1 (EC:3.1.3.2)
    Alternative name(s):
    Manganese(II) purple acid phosphatase 1
    Gene namesi
    Name:PAP1
    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 – 3838Sequence AnalysisAdd
    BLAST
    Chaini39 – 473435Purple acid phosphatase 1PRO_5000057351Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi118 – 1181N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi180 – 1801N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi311 – 3111N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi382 – 382InterchainBy similarity
    Glycosylationi433 – 4331N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked.By similarity

    Structurei

    Secondary structure

    1
    473
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi42 – 454Combined sources
    Helixi52 – 543Combined sources
    Beta strandi64 – 707Combined sources
    Beta strandi72 – 765Combined sources
    Beta strandi78 – 869Combined sources
    Turni89 – 924Combined sources
    Beta strandi93 – 986Combined sources
    Beta strandi105 – 1084Combined sources
    Beta strandi110 – 1123Combined sources
    Beta strandi123 – 1297Combined sources
    Beta strandi137 – 1426Combined sources
    Helixi145 – 1473Combined sources
    Beta strandi149 – 1546Combined sources
    Beta strandi165 – 1706Combined sources
    Helixi177 – 18812Combined sources
    Beta strandi194 – 1985Combined sources
    Helixi205 – 2073Combined sources
    Helixi209 – 2113Combined sources
    Helixi214 – 22714Combined sources
    Helixi238 – 2403Combined sources
    Helixi245 – 2473Combined sources
    Helixi254 – 2596Combined sources
    Helixi265 – 2673Combined sources
    Beta strandi274 – 2796Combined sources
    Beta strandi282 – 2865Combined sources
    Helixi298 – 30912Combined sources
    Turni312 – 3143Combined sources
    Beta strandi317 – 3215Combined sources
    Turni332 – 3376Combined sources
    Helixi338 – 35013Combined sources
    Beta strandi354 – 3585Combined sources
    Beta strandi360 – 3678Combined sources
    Beta strandi369 – 3713Combined sources
    Beta strandi392 – 3965Combined sources
    Beta strandi417 – 4215Combined sources
    Beta strandi425 – 4317Combined sources
    Beta strandi433 – 44311Combined sources
    Beta strandi452 – 4587Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XZWX-ray2.50A/B39-464[»]
    ProteinModelPortaliQ9SE00.
    SMRiQ9SE00. Positions 39-464.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9SE00.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni360 – 3623Substrate 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.

    Q9SE00-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRLVVVGLWC LILGLILNPT KFCDAGVTSS YVRKSLSALP NAEDVDMPWD
    60 70 80 90 100
    SDVFAVPSGY NAPQQVHITQ GDYEGRGVII SWTTPYDKAG ANKVVYWSEN
    110 120 130 140 150
    SKSQKRAMGT VVTYKYYNYT SAFIHHCTIK DLEYDTKYYY RLGFGDAKRQ
    160 170 180 190 200
    FWFVTPPKPG PDVPYVFGLI GDIGQTHDSN TTLTHYEQNS AKGQAVLFMG
    210 220 230 240 250
    DLSYSNRWPN HDNNRWDTWG RFSERSVAYQ PWIWTAGNHE IDYAPDIGEY
    260 270 280 290 300
    QPFVPFTNRY PTPHEASGSG DPLWYAIKRA SAHIIVLSSY SGFVKYSPQY
    310 320 330 340 350
    KWFTSELEKV NRSETPWLIV LVHAPLYNSY EAHYMEGEAM RAIFEPYFVY
    360 370 380 390 400
    YKVDIVFSGH VHSYERSERV SNVAYNIVNA KCTPVSDESA PVYITIGDGG
    410 420 430 440 450
    NSEGLASEMT QPQPSYSAFR EASFGHGIFD IKNRTHAHFS WHRNQDGASV
    460 470
    EADSLWLLNR YWASEDASSM SAM
    Length:473
    Mass (Da):53,815
    Last modified:May 1, 2000 - v1
    Checksum:iBAE4B807DADD95A7
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF200825 mRNA. Translation: AAF19821.1.
    PIRiA59200.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF200825 mRNA. Translation: AAF19821.1.
    PIRiA59200.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XZWX-ray2.50A/B39-464[»]
    ProteinModelPortaliQ9SE00.
    SMRiQ9SE00. Positions 39-464.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-15153.
    BRENDAi3.1.3.2. 2773.

    Miscellaneous databases

    EvolutionaryTraceiQ9SE00.

    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.
    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.

    Entry informationi

    Entry nameiPPAF1_IPOBA
    AccessioniPrimary (citable) accession number: Q9SE00
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 5, 2009
    Last sequence update: May 1, 2000
    Last modified: May 27, 2015
    This is version 66 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    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.