Q8X176 · PHOA_ASPFU
- ProteinAcid phosphatase
- GenephoA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids447 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Has both phosphomonoesterase and phosphodiesterase activity. Cleaves a broad range of phosphate esters.
Catalytic activity
- a phosphate monoester + H2O = an alcohol + phosphate
Activity regulation
Inhibited by NaF, molybdate and vanadate.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
1.45 mM | p-nitrophenyl phosphate | |||||
2.3 mM | bis-(p-nitrophenyl) phosphate |
pH Dependence
Optimum pH is 4-6. Active from pH 3 to 7.
Features
Showing features for active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 215 | Proton donor | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Cellular Component | side of membrane | |
Molecular Function | acid phosphatase activity | |
Biological Process | cell wall organization | |
Biological Process | phospholipid catabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAcid phosphatase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Fumigati
Accessions
- Primary accessionQ8X176
- Secondary accessions
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, glycosylation, lipidation, propeptide.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-17 | ||||
Chain | PRO_0000245560 | 18-419 | Acid phosphatase | ||
Glycosylation | 119 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 150 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 177 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 186 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 208 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 217 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 234 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 240 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 315 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 332 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 382 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 405 | N-linked (GlcNAc...) asparagine | |||
Lipidation | 419 | GPI-like-anchor amidated serine | |||
Propeptide | PRO_0000245561 | 420-447 | Removed in mature form | ||
Post-translational modification
The GPI-like anchor contains a phosphoceramide lipid group. The anchor position has not been determined.
Keywords
- PTM
PTM databases
Expression
Induction
Repressed by phosphate.
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length447
- Mass (Da)48,988
- Last updated2002-03-01 v1
- MD5 Checksum572FA219DE776A2C3F50CF8511837015
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Sequence conflict | 329 | in Ref. 3; AA sequence | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF462065 EMBL· GenBank· DDBJ | AAL66381.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAHF01000007 EMBL· GenBank· DDBJ | EAL88069.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. |