Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Acid phosphatase

Schizophyllum commune (Split gill fungus)
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli


Catalytic activityi

A phosphate monoester + H2O = an alcohol + phosphate.1 Publication

Enzyme regulationi

Activated slightly by Co2+, Ca2+ and Mg2+. Strongly inhibited by NaF, Fe3+ and Al3+, less so by tartrate, Cu2+ and Hg+. Not affected by EDTA, Fe2+ and Zn2+.1 Publication


  1. KM=248 µM for para-nitrophenylphosphate (p-NPP)1 Publication
  1. Vmax=9 nM/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 4.6. Activity decreases sharply with decreases and increases in pH and is absent at pH 8.0. When pre-incubated at different pH levels, activity is stable between pH 4 and 9.1 Publication

Temperature dependencei

Optimum temperature is 50 degrees Celsius. Activity decreases sharply with decreases and increases in temperature. When pre-incubated at different temperatures, activity is stable between 20 and 50 degrees Celsius.1 Publication

GO - Molecular functioni

  • acid phosphatase activity Source: UniProtKB

GO - Biological processi

  • dephosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni


Names & Taxonomyi

Protein namesi
Recommended name:
Acid phosphatase1 Publication (EC: Publication)
OrganismiSchizophyllum commune (Split gill fungus)
Taxonomic identifieri5334 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesSchizophyllaceaeSchizophyllum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›10›10Acid phosphatasePRO_0000415411


Subunit structurei

Monomer.1 Publication


Sequence statusi: Fragment.

Mass (Da):1,142
Last modified:January 25, 2012 - v1

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei10 – 1011 Publication


3D structure databases


Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases


Entry informationi

Entry nameiPPA_SCHCO
AccessioniPrimary (citable) accession number: B3EWC6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: January 25, 2012
Last modified: November 11, 2015
This is version 7 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program



Has no activity towards sodium phytate, ATP, ADP, AMP, glucose-6-phosphate, fructose-6-phosphate and beta-glycerophosphate.1 Publication

Keywords - Technical termi

Direct protein sequencing

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.