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P81440

- PHYB_ASPFI

UniProt

P81440 - PHYB_ASPFI

Protein

3-phytase B

Gene

phyB

Organism
Aspergillus ficuum
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Catalyzes the hydrolysis of inorganic orthophosphate from phytate.

    Catalytic activityi

    Myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei17 – 171NucleophileBy similarity

    GO - Molecular functioni

    1. 3-phytase activity Source: UniProtKB-EC
    2. acid phosphatase activity Source: InterPro

    Keywords - Molecular functioni

    Hydrolase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-phytase B (EC:3.1.3.8)
    Alternative name(s):
    3 phytase B
    Myo-inositol hexakisphosphate phosphohydrolase B
    Myo-inositol-hexaphosphate 3-phosphohydrolase B
    Gene namesi
    Name:phyB
    OrganismiAspergillus ficuum
    Taxonomic identifieri5058 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – ›28›283-phytase BPRO_0000114471Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP81440.
    SMRiP81440. Positions 1-28.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidine acid phosphatase family.Curated

    Family and domain databases

    InterProiIPR000560. His_Pase_superF_clade-2.
    IPR029033. His_PPase_superfam.
    [Graphical view]
    SUPFAMiSSF53254. SSF53254. 1 hit.
    PROSITEiPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Fragment.

    P81440-1 [UniParc]FASTAAdd to Basket

    « Hide

    RDPTGCEVDQ VIMVKRHGER YPSPSAGK                           28
    Length:28
    Mass (Da):3,114
    Last modified:December 15, 1998 - v1
    Checksum:i675340A707C57CD8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11
    Non-terminal residuei28 – 281

    Sequence databases

    PIRiJN0715.

    Cross-referencesi

    Sequence databases

    PIRi JN0715.

    3D structure databases

    ProteinModelPortali P81440.
    SMRi P81440. Positions 1-28.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    InterProi IPR000560. His_Pase_superF_clade-2.
    IPR029033. His_PPase_superfam.
    [Graphical view ]
    SUPFAMi SSF53254. SSF53254. 1 hit.
    PROSITEi PS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of active-site residues in Aspergillus ficuum extracellular pH 2.5 optimum acid phosphatase."
      Ullah A.H., Dischinger H.C. Jr.
      Biochem. Biophys. Res. Commun. 192:754-759(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.

    Entry informationi

    Entry nameiPHYB_ASPFI
    AccessioniPrimary (citable) accession number: P81440
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: December 15, 1998
    Last modified: October 1, 2014
    This is version 54 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3