O00100 · PHYA2_ASPTE
- ProteinPhytase A
- GenephyA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids466 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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 + phosphateThis reaction proceeds in the forward direction.
- 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + H2O = 1D-myo-inositol 1,2,5,6-tetrakisphosphate + phosphateThis reaction proceeds in the forward direction.
- 1D-myo-inositol 1,2,5,6-tetrakisphosphate + H2O = 1D-myo-inositol 1,2,6-trisphosphate + phosphateThis reaction proceeds in the forward direction.
- 1D-myo-inositol 1,2,6-trisphosphate + H2O = 1D-myo-inositol 1,2-bisphosphate + phosphateThis reaction proceeds in the forward direction.
- 1D-myo-inositol 1,2-bisphosphate + H2O = 1D-myo-inositol 2-phosphate + phosphateThis reaction proceeds in the forward direction.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
23.2 μM | phytate |
pH Dependence
Optimum pH is 5.5. Active from 4 to 6.5.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 51 | 1D-myo-inositol hexakisphosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 81 | 1D-myo-inositol hexakisphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 82 | Nucleophile | ||||
Sequence: H | ||||||
Binding site | 82 | 1D-myo-inositol hexakisphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 85 | 1D-myo-inositol hexakisphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 88 | 1D-myo-inositol hexakisphosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 165 | 1D-myo-inositol hexakisphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 301 | 1D-myo-inositol hexakisphosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 361 | 1D-myo-inositol hexakisphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 362 | 1D-myo-inositol hexakisphosphate (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | 3-phytase activity | |
Molecular Function | acid phosphatase activity |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhytase A
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Circumdati
Accessions
- Primary accessionO00100
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MGVFVVLLSIATLFGSTSG | ||||||
Chain | PRO_0000283712 | 20-466 | Phytase A | |||
Sequence: TALGPRGNHSDCTSVDRGYQCFPELSHKWGLYAPYFSLQDESPFPLDVPDDCHITFVQVLARHGARSPTDSKTKAYAATIAAIQKNATALPGKYAFLKSYNYSMGSENLNPFGRNQLQDLGAQFYRRYDTLTRHINPFVRAADSSRVHESAEKFVEGFQNARQGDPHANPHQPSPRVDVVIPEGTAYNNTLEHSICTAFEASTVGDAAADNFTAVFAPAIAKRLEADLPGVQLSADDVVNLMAMCPFETVSLTDDAHTLSPFCDLFTAAEWTQYNYLLSLDKYYGYGGGNPLGPVQGVGWANELIARLTRSPVHDHTCVNNTLDANPATFPLNATLYADFSHDSNLVSIFWALGLYNGTKPLSQTTVEDITRTDGYAAAWTVPFAARAYIEMMQCRAEKQPLVRVLVNDRVMPLHGCAVDNLGRCKRDDFVEGLSFARAGGNWAECF | ||||||
Glycosylation | 27 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 31↔40 | |||||
Sequence: CTSVDRGYQC | ||||||
Disulfide bond | 71↔414 | |||||
Sequence: CHITFVQVLARHGARSPTDSKTKAYAATIAAIQKNATALPGKYAFLKSYNYSMGSENLNPFGRNQLQDLGAQFYRRYDTLTRHINPFVRAADSSRVHESAEKFVEGFQNARQGDPHANPHQPSPRVDVVIPEGTAYNNTLEHSICTAFEASTVGDAAADNFTAVFAPAIAKRLEADLPGVQLSADDVVNLMAMCPFETVSLTDDAHTLSPFCDLFTAAEWTQYNYLLSLDKYYGYGGGNPLGPVQGVGWANELIARLTRSPVHDHTCVNNTLDANPATFPLNATLYADFSHDSNLVSIFWALGLYNGTKPLSQTTVEDITRTDGYAAAWTVPFAARAYIEMMQC | ||||||
Glycosylation | 105 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 120 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 207 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 215↔465 | |||||
Sequence: CTAFEASTVGDAAADNFTAVFAPAIAKRLEADLPGVQLSADDVVNLMAMCPFETVSLTDDAHTLSPFCDLFTAAEWTQYNYLLSLDKYYGYGGGNPLGPVQGVGWANELIARLTRSPVHDHTCVNNTLDANPATFPLNATLYADFSHDSNLVSIFWALGLYNGTKPLSQTTVEDITRTDGYAAAWTVPFAARAYIEMMQCRAEKQPLVRVLVNDRVMPLHGCAVDNLGRCKRDDFVEGLSFARAGGNWAEC | ||||||
Glycosylation | 230 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 264↔282 | |||||
Sequence: CPFETVSLTDDAHTLSPFC | ||||||
Glycosylation | 339 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 352 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 376 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 436↔444 | |||||
Sequence: CAVDNLGRC |
Keywords
- PTM
PTM databases
Interaction
Subunit
Monomer.
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length466
- Mass (Da)51,055
- Last updated1997-07-01 v1
- ChecksumF2AECEC1AF7C22C4
Keywords
- Technical term