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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)DescriptionActionsGraphical viewLength
    Metal bindingi172IronBy similarity1
    Metal bindingi201IronBy similarity1
    Metal bindingi201Manganese1
    Metal bindingi204IronBy similarity1
    Metal bindingi238Manganese1
    Binding sitei238SubstrateBy similarity1
    Metal bindingi323Manganese1
    Active sitei333Proton donorBy similarity1
    Metal bindingi360Manganese1
    Metal bindingi362IronBy similarity1

    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)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 38Sequence analysisAdd BLAST38
    ChainiPRO_500005735139 – 473Purple acid phosphatase 1Add BLAST435

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Glycosylationi118N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi180N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi311N-linked (GlcNAc...)Sequence analysis1
    Disulfide bondi382InterchainBy similarity
    Glycosylationi433N-linked (GlcNAc...)Sequence analysis1

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked.By similarity

    Structurei

    Secondary structure

    1473
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi42 – 45Combined sources4
    Helixi52 – 54Combined sources3
    Beta strandi64 – 70Combined sources7
    Beta strandi72 – 76Combined sources5
    Beta strandi78 – 86Combined sources9
    Turni89 – 92Combined sources4
    Beta strandi93 – 98Combined sources6
    Beta strandi105 – 108Combined sources4
    Beta strandi110 – 112Combined sources3
    Beta strandi123 – 129Combined sources7
    Beta strandi137 – 142Combined sources6
    Helixi145 – 147Combined sources3
    Beta strandi149 – 154Combined sources6
    Beta strandi165 – 170Combined sources6
    Helixi177 – 188Combined sources12
    Beta strandi194 – 198Combined sources5
    Helixi205 – 207Combined sources3
    Helixi209 – 211Combined sources3
    Helixi214 – 227Combined sources14
    Helixi238 – 240Combined sources3
    Helixi245 – 247Combined sources3
    Helixi254 – 259Combined sources6
    Helixi265 – 267Combined sources3
    Beta strandi274 – 279Combined sources6
    Beta strandi282 – 286Combined sources5
    Helixi298 – 309Combined sources12
    Turni312 – 314Combined sources3
    Beta strandi317 – 321Combined sources5
    Turni332 – 337Combined sources6
    Helixi338 – 350Combined sources13
    Beta strandi354 – 358Combined sources5
    Beta strandi360 – 367Combined sources8
    Beta strandi369 – 371Combined sources3
    Beta strandi392 – 396Combined sources5
    Beta strandi417 – 421Combined sources5
    Beta strandi425 – 431Combined sources7
    Beta strandi433 – 443Combined sources11
    Beta strandi452 – 458Combined sources7

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiQ9SE00.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni360 – 362Substrate bindingBy similarity3

    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.
    PF16656. Pur_ac_phosph_N. 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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1XZWX-ray2.50A/B39-464[»]
    ProteinModelPortaliQ9SE00.
    SMRiQ9SE00.
    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.
    PF16656. Pur_ac_phosph_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF49363. SSF49363. 1 hit.
    SSF56300. SSF56300. 1 hit.
    ProtoNetiSearch...

    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: November 30, 2016
    This is version 72 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

    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 one 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.