P34753 · PHYA_ASPAW

Function

function

Catalyzes the phosphate monoester hydrolysis of phytic acid (myo-inositol hexakisphosphate), which results in the stepwise formation of myo-inositol pentakis-, tetrakis-, tris-, bis-, and monophosphates, as well as the liberation of inorganic phosphate (PubMed:8224894).
Myo-inositol 2-monophosphate is the end product (By similarity).

Catalytic activity

  • 1D-myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
    This reaction proceeds in the forward direction.
    EC:3.1.3.8 (UniProtKB | ENZYME | Rhea)
  • 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + H2O = 1D-myo-inositol 1,2,5,6-tetrakisphosphate + phosphate
    This reaction proceeds in the forward direction.
  • 1D-myo-inositol 1,2,5,6-tetrakisphosphate + H2O = 1D-myo-inositol 1,2,6-trisphosphate + phosphate
    This reaction proceeds in the forward direction.
  • 1D-myo-inositol 1,2,6-trisphosphate + H2O = 1D-myo-inositol 1,2-bisphosphate + phosphate
    This reaction proceeds in the forward direction.
  • 1D-myo-inositol 1,2-bisphosphate + H2O = 1D-myo-inositol 2-phosphate + phosphate
    This reaction proceeds in the forward direction.

Biotechnology

Phytic acid is the major storage form of phosphorus in plant seeds and, thus, in seed-based animal feed. Phytases are therefore of considerable economic interest.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site501D-myo-inositol hexakisphosphate (UniProtKB | ChEBI)
Binding site511D-myo-inositol hexakisphosphate (UniProtKB | ChEBI)
Binding site811D-myo-inositol hexakisphosphate (UniProtKB | ChEBI)
Active site82Nucleophile
Binding site821D-myo-inositol hexakisphosphate (UniProtKB | ChEBI)
Binding site851D-myo-inositol hexakisphosphate (UniProtKB | ChEBI)
Binding site881D-myo-inositol hexakisphosphate (UniProtKB | ChEBI)
Binding site1651D-myo-inositol hexakisphosphate (UniProtKB | ChEBI)
Binding site3011D-myo-inositol hexakisphosphate (UniProtKB | ChEBI)
Binding site3611D-myo-inositol hexakisphosphate (UniProtKB | ChEBI)
Binding site3621D-myo-inositol hexakisphosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentextracellular region
Molecular Function3-phytase activity
Molecular Functionacid phosphatase activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Phytase A
  • EC number
  • Alternative names
    • Histidine acid phosphatase phyA
      (HAP
      )
    • Myo-inositol hexakisphosphate phosphohydrolase A
    • Myo-inositol-hexaphosphate 3-phosphohydrolase A

Gene names

    • Name
      phyA
    • Synonyms
      phy

Organism names

  • Taxonomic identifier
  • Strain
    • ALK0243
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus

Accessions

  • Primary accession
    P34753

Subcellular Location

Keywords

Phenotypes & Variants

PTM/Processing

Features

Showing features for signal, chain, glycosylation, disulfide bond.

TypeIDPosition(s)Description
Signal1-23
ChainPRO_000002397124-467Phytase A
Glycosylation27N-linked (GlcNAc...) asparagine
Disulfide bond31↔40
Glycosylation59N-linked (GlcNAc...) asparagine
Disulfide bond71↔414
Glycosylation105N-linked (GlcNAc...) asparagine
Glycosylation120N-linked (GlcNAc...) asparagine
Glycosylation207N-linked (GlcNAc...) asparagine
Disulfide bond215↔465
Glycosylation230N-linked (GlcNAc...) asparagine
Disulfide bond264↔282
Glycosylation339N-linked (GlcNAc...) asparagine
Glycosylation352N-linked (GlcNAc...) asparagine
Glycosylation376N-linked (GlcNAc...) asparagine
Glycosylation388N-linked (GlcNAc...) asparagine
Disulfide bond436↔444

Keywords

PTM databases

Interaction

Subunit

Monomer.

Structure

Family & Domains

Sequence similarities

Belongs to the histidine acid phosphatase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    467
  • Mass (Da)
    51,075
  • Last updated
    1994-02-01 v1
  • Checksum
    118E828A5D7EC661
MGVSAVLLPLYLLAGVTSGLAVPASRNQSTCDTVDQGYQCFSETSHLWGQYAPFFSLANESAISPDVPAGCRVTFAQVLSRHGARYPTESKGKKYSALIEEIQQNVTTFDGKYAFLKTYNYSLGADDLTPFGEQELVNSGIKFYQRYESLTRNIIPFIRSSGSSRVIASGEKFIEGFQSTKLKDPRAQPGQSSPKIDVVISEASSSNNTLDPGTCTVFEDSELADTVEANFTATFAPSIRQRLENDLSGVTLTDTEVTYLMDMCSFDTISTSTVDTKLSPFCDLFTHDEWIHYDYLQSLKKYYGHGAGNPLGPTQGVGYANELIARLTHSPVHDDTSSNHTLDSNPATFPLNSTLYADFSHDNGIISILFALGLYNGTKPLSTTTVENITQTDGFSSAWTVPFASRLYVEMMQCQAEQEPLVRVLVNDRVVPLHGCPIDALGRCTRDSFVRGLSFARSGGDWAECSA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
L02421
EMBL· GenBank· DDBJ
AAA16898.1
EMBL· GenBank· DDBJ
Unassigned DNA

Similar Proteins

Disclaimer

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