P34753 · PHYA_ASPAW
- ProteinPhytase A
- GenephyA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids467 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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:8224894).
Myo-inositol 2-monophosphate is the end product (By similarity).
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 + 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.
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 50 | 1D-myo-inositol hexakisphosphate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
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
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus
Accessions
- Primary accessionP34753
Subcellular Location
Phenotypes & Variants
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-23 | |||||
Sequence: MGVSAVLLPLYLLAGVTSGLAVP | ||||||
Chain | PRO_0000023971 | 24-467 | Phytase A | |||
Sequence: ASRNQSTCDTVDQGYQCFSETSHLWGQYAPFFSLANESAISPDVPAGCRVTFAQVLSRHGARYPTESKGKKYSALIEEIQQNVTTFDGKYAFLKTYNYSLGADDLTPFGEQELVNSGIKFYQRYESLTRNIIPFIRSSGSSRVIASGEKFIEGFQSTKLKDPRAQPGQSSPKIDVVISEASSSNNTLDPGTCTVFEDSELADTVEANFTATFAPSIRQRLENDLSGVTLTDTEVTYLMDMCSFDTISTSTVDTKLSPFCDLFTHDEWIHYDYLQSLKKYYGHGAGNPLGPTQGVGYANELIARLTHSPVHDDTSSNHTLDSNPATFPLNSTLYADFSHDNGIISILFALGLYNGTKPLSTTTVENITQTDGFSSAWTVPFASRLYVEMMQCQAEQEPLVRVLVNDRVVPLHGCPIDALGRCTRDSFVRGLSFARSGGDWAECSA | ||||||
Glycosylation | 27 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 31↔40 | |||||
Sequence: CDTVDQGYQC | ||||||
Glycosylation | 59 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 71↔414 | |||||
Sequence: CRVTFAQVLSRHGARYPTESKGKKYSALIEEIQQNVTTFDGKYAFLKTYNYSLGADDLTPFGEQELVNSGIKFYQRYESLTRNIIPFIRSSGSSRVIASGEKFIEGFQSTKLKDPRAQPGQSSPKIDVVISEASSSNNTLDPGTCTVFEDSELADTVEANFTATFAPSIRQRLENDLSGVTLTDTEVTYLMDMCSFDTISTSTVDTKLSPFCDLFTHDEWIHYDYLQSLKKYYGHGAGNPLGPTQGVGYANELIARLTHSPVHDDTSSNHTLDSNPATFPLNSTLYADFSHDNGIISILFALGLYNGTKPLSTTTVENITQTDGFSSAWTVPFASRLYVEMMQC | ||||||
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: CTVFEDSELADTVEANFTATFAPSIRQRLENDLSGVTLTDTEVTYLMDMCSFDTISTSTVDTKLSPFCDLFTHDEWIHYDYLQSLKKYYGHGAGNPLGPTQGVGYANELIARLTHSPVHDDTSSNHTLDSNPATFPLNSTLYADFSHDNGIISILFALGLYNGTKPLSTTTVENITQTDGFSSAWTVPFASRLYVEMMQCQAEQEPLVRVLVNDRVVPLHGCPIDALGRCTRDSFVRGLSFARSGGDWAEC | ||||||
Glycosylation | 230 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 264↔282 | |||||
Sequence: CSFDTISTSTVDTKLSPFC | ||||||
Glycosylation | 339 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 352 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 376 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 388 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 436↔444 | |||||
Sequence: CPIDALGRC |
Keywords
- PTM
PTM databases
Interaction
Subunit
Monomer.
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length467
- Mass (Da)51,075
- Last updated1994-02-01 v1
- Checksum118E828A5D7EC661