O00100 · PHYA2_ASPTE

  • Protein
    Phytase A
  • Gene
    phyA
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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:9925555).
Myo-inositol 2-monophosphate is the end product (PubMed:9925555).
Has a broad substrate specificity and is also able to dephosphorylate other classic acid phosphatase substrates such as p-nitrophenyl phosphate, phenyl phosphate, fructose 1,6-bisphosphate, glucose 6-phosphate, 3-phosphoglycerate, as well as ADP and ATP (PubMed:9925555).

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.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
23.2 μMphytate

pH Dependence

Optimum pH is 5.5. Active from 4 to 6.5.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
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

Organism names

  • Taxonomic identifier
  • Strain
    • ATCC 10020 / NRRL 1960 / CBS 116.46 / IFO 6123 / DSM 826 / IMI 44243
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Circumdati

Accessions

  • Primary accession
    O00100

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

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

TypeIDPosition(s)Description
Signal1-19
ChainPRO_000028371220-466Phytase A
Glycosylation27N-linked (GlcNAc...) asparagine
Disulfide bond31↔40
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
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
    466
  • Mass (Da)
    51,055
  • Last updated
    1997-07-01 v1
  • Checksum
    F2AECEC1AF7C22C4
MGVFVVLLSIATLFGSTSGTALGPRGNHSDCTSVDRGYQCFPELSHKWGLYAPYFSLQDESPFPLDVPDDCHITFVQVLARHGARSPTDSKTKAYAATIAAIQKNATALPGKYAFLKSYNYSMGSENLNPFGRNQLQDLGAQFYRRYDTLTRHINPFVRAADSSRVHESAEKFVEGFQNARQGDPHANPHQPSPRVDVVIPEGTAYNNTLEHSICTAFEASTVGDAAADNFTAVFAPAIAKRLEADLPGVQLSADDVVNLMAMCPFETVSLTDDAHTLSPFCDLFTAAEWTQYNYLLSLDKYYGYGGGNPLGPVQGVGWANELIARLTRSPVHDHTCVNNTLDANPATFPLNATLYADFSHDSNLVSIFWALGLYNGTKPLSQTTVEDITRTDGYAAAWTVPFAARAYIEMMQCRAEKQPLVRVLVNDRVMPLHGCAVDNLGRCKRDDFVEGLSFARAGGNWAECF

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U60412
EMBL· GenBank· DDBJ
AAB58465.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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