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Q9SE00

- PPAF1_IPOBA

UniProt

Q9SE00 - PPAF1_IPOBA

Protein

Purple acid phosphatase 1

Gene

PAP1

Organism
Ipomoea batatas (Sweet potato) (Convolvulus batatas)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 61 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Cofactori

    Binds 1 iron ion per subunit.By similarity
    Binds 1 manganese ion per subunit. Can also use zinc, copper and magnesium ions.1 Publication

    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

    1. acid phosphatase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Iron, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-15153.

    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

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    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 – 454
    Helixi52 – 543
    Beta strandi64 – 707
    Beta strandi72 – 765
    Beta strandi78 – 869
    Turni89 – 924
    Beta strandi93 – 986
    Beta strandi105 – 1084
    Beta strandi110 – 1123
    Beta strandi123 – 1297
    Beta strandi137 – 1426
    Helixi145 – 1473
    Beta strandi149 – 1546
    Beta strandi165 – 1706
    Helixi177 – 18812
    Beta strandi194 – 1985
    Helixi205 – 2073
    Helixi209 – 2113
    Helixi214 – 22714
    Helixi238 – 2403
    Helixi245 – 2473
    Helixi254 – 2596
    Helixi265 – 2673
    Beta strandi274 – 2796
    Beta strandi282 – 2865
    Helixi298 – 30912
    Turni312 – 3143
    Beta strandi317 – 3215
    Turni332 – 3376
    Helixi338 – 35013
    Beta strandi354 – 3585
    Beta strandi360 – 3678
    Beta strandi369 – 3713
    Beta strandi392 – 3965
    Beta strandi417 – 4215
    Beta strandi425 – 4317
    Beta strandi433 – 44311
    Beta strandi452 – 4587

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MRLVVVGLWC LILGLILNPT KFCDAGVTSS YVRKSLSALP NAEDVDMPWD    50
    SDVFAVPSGY NAPQQVHITQ GDYEGRGVII SWTTPYDKAG ANKVVYWSEN 100
    SKSQKRAMGT VVTYKYYNYT SAFIHHCTIK DLEYDTKYYY RLGFGDAKRQ 150
    FWFVTPPKPG PDVPYVFGLI GDIGQTHDSN TTLTHYEQNS AKGQAVLFMG 200
    DLSYSNRWPN HDNNRWDTWG RFSERSVAYQ PWIWTAGNHE IDYAPDIGEY 250
    QPFVPFTNRY PTPHEASGSG DPLWYAIKRA SAHIIVLSSY SGFVKYSPQY 300
    KWFTSELEKV NRSETPWLIV LVHAPLYNSY EAHYMEGEAM RAIFEPYFVY 350
    YKVDIVFSGH VHSYERSERV SNVAYNIVNA KCTPVSDESA PVYITIGDGG 400
    NSEGLASEMT QPQPSYSAFR EASFGHGIFD IKNRTHAHFS WHRNQDGASV 450
    EADSLWLLNR YWASEDASSM SAM 473
    Length:473
    Mass (Da):53,815
    Last modified:May 1, 2000 - v1
    Checksum:iBAE4B807DADD95A7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF200825 mRNA. Translation: AAF19821.1.
    PIRiA59200.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF200825 mRNA. Translation: AAF19821.1 .
    PIRi A59200.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XZW X-ray 2.50 A/B 39-464 [» ]
    ProteinModelPortali Q9SE00.
    SMRi Q9SE00. Positions 39-464.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-15153.

    Miscellaneous databases

    EvolutionaryTracei Q9SE00.

    Family and domain databases

    Gene3Di 2.60.40.380. 1 hit.
    3.60.21.10. 1 hit.
    InterProi IPR004843. 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 ]
    Pfami PF00149. Metallophos. 1 hit.
    PF14008. Metallophos_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49363. SSF49363. 1 hit.
    SSF56300. SSF56300. 1 hit.
    ProtoNeti Search...

    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: October 1, 2014
    This is version 61 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