Reviewed,
UniProtKB/Swiss-Prot Q12546 (PPA_ASPFI)
Last modified
June 16, 2009.
Version 55.
History...
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information
Names and origin
| Protein names | Recommended name: Acid phosphatase EC=3.1.3.2 Alternative name(s): pH 6-optimum acid phosphatase APase6 | ||
| Gene names |
| ||
| Organism | Aspergillus ficuum | ||
| Taxonomic identifier | 5058 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus |
Protein attributes
| Sequence length | 614 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)
| Catalytic activity | A phosphate monoester + H2O = an alcohol + phosphate. |
| Cofactor | Copper Potential. |
| Enzyme regulation | Competitively inhibited by phosphomycin and inorganic orthophosphate. |
| Subunit structure | Monomer. |
| Subcellular location | |
| Post-translational modification | Glycosylated; probably with N-linked high-mannose oligosaccharides. |
| biophysicochemical properties | pH dependence: Optimum pH is 6. Inactive above pH 6.7. Temperature dependence: Optimum temperature is 63 degrees Celsius. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Domain | Signal |
| Ligand | Copper |
| Molecular function | Hydrolase |
| PTM | Glycoprotein |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | acid phosphatase activity Inferred from electronic annotation. Source: EC copper ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 22 | 22 | Ref.2 Ref.3 | ||||||
| Chain | 23 – 605 | 583 | Acid phosphatase | PRO_0000023997 | |||||
| Propeptide | 606 – 614 | 9 | PRO_0000023998 | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 110 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 161 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 242 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 295 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 333 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 340 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 352 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 408 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 429 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 512 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 523 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 559 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 578 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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References
| [1] | "The Aspergillus niger (ficuum) aphA gene encodes a pH 6.0-optimum acid phosphatase." Mullaney E.J., Daly C.B., Ehrlich K.C., Ullah A.H.J. Gene 162:117-121(1995) [PubMed: 7557398] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 66876 / DSM 932 / SRRC 265 / NRRL 3135. |
| [2] | "The complete primary structure elucidation of Aspergillus ficuum (niger), pH 6.0, optimum acid phosphatase by Edman degradation." Ullah A.H.J., Mullaney E.M., Dischinger H.C. Jr. Biochem. Biophys. Res. Commun. 203:182-189(1994) [PubMed: 8074654] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-605. Strain: ATCC 66876 / DSM 932 / SRRC 265 / NRRL 3135. |
| [3] | "Aspergillus ficuum extracellular pH 6.0 optimum acid phosphatase: purification, N-terminal amino acid sequence, and biochemical characterization." Ullah A.H.J., Cummins B.J. Prep. Biochem. 18:37-65(1988) [PubMed: 3375203] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-56, CHARACTERIZATION. Strain: ATCC 66876 / DSM 932 / SRRC 265 / NRRL 3135. |
Cross-references
Sequence databases | |
|---|---|
| U18553 Genomic DNA. Translation: AAA91632.1. | |
| PIR | JC2545. |
3D structure databases | |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 3.1.3.2. 81696. |
Family and domain databases | |
| InterPro | IPR014390. Acid_Pase_Asper. IPR003961. FN_III. IPR004843. M-pesterase. IPR015914. Purple_acid_Pase_N. [Graphical view] |
| Gene3D | G3DSA:2.60.40.380. Purple_acid_Pase_N. 1 hit. |
| Pfam | PF00149. Metallophos. 1 hit. [Graphical view] |
| PIRSF | PIRSF000900. Acid_Ptase_Asper. 1 hit. |
| SMART | SM00060. FN3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PPA_ASPFI | ||||||||
| Accession | Primary (citable) accession number: Q12546 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||

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