O00085 (PHYA1_ASPTE) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 60.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: 3-phytase A EC=3.1.3.8 Alternative name(s): 3 phytase A Myo-inositol hexakisphosphate phosphohydrolase A Myo-inositol-hexaphosphate 3-phosphohydrolase A | ||
| Gene names |
| ||
| Organism | Aspergillus terreus | ||
| Taxonomic identifier | 33178 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus![]() |
Protein attributes
| Sequence length | 466 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Catalyzes the hydrolysis of inorganic orthophosphate from phytate. Releases 5 of the 6 phosphate groups to yield the end product myo-inositol 2-monophosphate. Specific for phytate. Ref.3 |
| Catalytic activity | Myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate. |
| Subunit structure | Monomer. Ref.2 |
| Subcellular location | |
| Sequence similarities | Belongs to the histidine acid phosphatase family. |
| Biophysicochemical properties | Kinetic parameters: KM=10.6 µM for phytate Ref.3 pH dependence: Optimum pH is 5.5. Active from 2.5 to 7.5 with phytic acid as substrate. The optimum pH is shifted to more acidic values with 4-nitrophenyl phosphate as substrate. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Hydrolase |
| PTM | Disulfide bond Glycoprotein |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | dephosphorylation Inferred from electronic annotation. Source: GOC |
| Cellular_component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | 3-phytase activity Inferred from electronic annotation. Source: EC acid phosphatase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 19 | 19 | By similarity | ||||||||
| Chain | 20 – 466 | 447 | 3-phytase A | PRO_0000023972 | |||||||
Sites | |||||||||||
| Active site | 82 | 1 | Nucleophile By similarity | ||||||||
| Active site | 362 | 1 | Proton donor By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 120 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 207 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 230 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 339 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 352 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 376 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 31 ↔ 40 | By similarity | |||||||||
| Disulfide bond | 71 ↔ 414 | By similarity | |||||||||
| Disulfide bond | 215 ↔ 465 | By similarity | |||||||||
| Disulfide bond | 264 ↔ 282 | By similarity | |||||||||
| Disulfide bond | 436 ↔ 444 | By similarity | |||||||||
Sequences
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References
| [1] | "The phytase subfamily of histidine acid phosphatases: isolation of genes for two novel phytases from the fungi Aspergillus terreus and Myceliophthora thermophila." Mitchell D.B., Vogel K., Weimann B.J., Pasamontes L., van Loon A.P.G.M. Microbiology 143:245-252(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION. Strain: 9A1. |
| [2] | "Biophysical characterization of fungal phytases (myo-inositol hexakisphosphate phosphohydrolases): molecular size, glycosylation pattern, and engineering of proteolytic resistance." Wyss M., Pasamontes L., Friedlein A., Remy R., Tessier M., Kronenberger A., Middendorf A., Lehmann M., Schnoebelen L., Roethlisberger U., Kusznir E., Wahl G., Mueller F., Lahm H.-W., Vogel K., van Loon A.P.G.M. Appl. Environ. Microbiol. 65:359-366(1999) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 29-38 AND 192-200, SUBUNIT. Strain: 9A1. |
| [3] | "Biochemical characterization of fungal phytases (myo-inositol hexakisphosphate phosphohydrolases): catalytic properties." Wyss M., Brugger R., Kronenberger A., Remy R., Fimbel R., Oesterhelt G., Lehmann M., van Loon A.P.G.M. Appl. Environ. Microbiol. 65:367-373(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U59805 Genomic DNA. Translation: AAB52507.1. |
3D structure databases | |
| ProteinModelPortal | O00085. |
| SMR | O00085. Positions 31-466. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Enzyme and pathway databases | |
| BRENDA | 3.1.3.8. 536. |
Family and domain databases | |
| InterPro | IPR000560. His_Pase_superF_clade-2. IPR016274. Histidine_acid_Pase_euk. [Graphical view] |
| Pfam | PF00328. His_Phos_2. 1 hit. [Graphical view] |
| PIRSF | PIRSF000894. Acid_phosphatase. 1 hit. |
| PROSITE | PS00616. HIS_ACID_PHOSPHAT_1. 1 hit. PS00778. HIS_ACID_PHOSPHAT_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PHYA1_ASPTE | ||||||||
| Accession | Primary (citable) accession number: O00085 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
