P34753 (PHYA_ASPAW) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 67.
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 awamori (Black koji mold) | ||||
| Taxonomic identifier | 105351 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus![]() |
Protein attributes
| Sequence length | 467 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the hydrolysis of inorganic orthophosphate from phytate. |
| Catalytic activity | Myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate. |
| Subcellular location | |
| Sequence similarities | Belongs to the histidine acid phosphatase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Hydrolase |
| PTM | Disulfide bond Glycoprotein |
| 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 – 23 | 23 | Potential | ||||||||
| Chain | 24 – 467 | 444 | 3-phytase A | PRO_0000023971 | |||||||
Sites | |||||||||||
| Active site | 82 | 1 | Nucleophile By similarity | ||||||||
| Active site | 362 | 1 | Proton donor By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 27 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 59 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 105 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| 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 | ||||||||
| Glycosylation | 388 | 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
| ||||||||||||||||||
References
| [1] | "The cloning and sequencing of the genes encoding phytase (phy) and pH 2.5-optimum acid phosphatase (aph) from Aspergillus niger var. awamori." Piddington C.S., Houston C.S., Paloheimo M.T., Cantrell M.A., Miettinen-Oinonen A., Nevalainen H., Rambosek J.A. Gene 133:55-62(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ALK0243. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L02421 Unassigned DNA. Translation: AAA16898.1. |
| PIR | JN0889. |
3D structure databases | |
| ProteinModelPortal | P34753. |
| SMR | P34753. Positions 30-467. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
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 | PHYA_ASPAW | ||||||||
| Accession | Primary (citable) accession number: P34753 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
