Detail Information for IndEnz0011000062
IED ID IndEnz0011000062
Enzyme Type ID glucanase000062
Protein Name Aspartic protease
EC 3.4.23.-
Gene Name pr1
Organism Phaffia rhodozyma (Yeast) (Xanthophyllomyces dendrorhous)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Agaricomycotina Tremellomycetes Cystofilobasidiales Mrakiaceae Phaffia Phaffia rhodozyma (Yeast) (Xanthophyllomyces dendrorhous)
Enzyme Sequence MISDTVIAILAVALVGSTVQAAPVDATATSTSGIIAVPISKSAAQLAREADPVVSLDWLKKTKAQAQYKHKQANARLHSKRATGASVLTDQGSESLWTGPITIGGQSFTVDWDTGSSDLWVPSSACSSAACNAHHKYTLTSTGKKQSGTFSISYGDGSSASGPVYKDNVVASGLQATSQVFGAVTSESSSFSSDPSDGISGLGWPALAQLSGTSYFWSLINQGTVTSPVFSFRLATTNSELYLGGINSAHYTGAITYTPVTQKAYWTIALGGVSVNGAAINPSVSSAIIDTGTTLVYGPTAGVAALYAKIPGSASMADTYGSDYQGYYTFPCSAVPTVALTFGGSSFSVPTSAFNLGTVSSGSKQCVGGIVGQGDGSWLVGDVFLQGVYSIYDVGNARVGFAKTV
Enzyme Length 405
Uniprot Accession Number O60020
Absorption
Active Site ACT_SITE 113; /evidence="ECO:0000250|UniProtKB:P00790, ECO:0000255|PROSITE-ProRule:PRU10094"; ACT_SITE 290; /evidence="ECO:0000250|UniProtKB:P00790, ECO:0000255|PROSITE-ProRule:PRU10094"
Activity Regulation ACTIVITY REGULATION: Inhibited by pepstatin A. {ECO:0000269|PubMed:10091328}.
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.23.-
Enzyme Function FUNCTION: Possesses acidic protease activity. Hydrolyzes casein and azoalbumin in vitro. {ECO:0000269|PubMed:10091328}.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is approximately 40 degrees Celsius. {ECO:0000269|PubMed:10091328};
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4-6. {ECO:0000269|PubMed:10091328};
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Disulfide bond (2); Domain (1); Propeptide (1); Signal peptide (1)
Keywords Aspartyl protease;Cleavage on pair of basic residues;Direct protein sequencing;Disulfide bond;Hydrolase;Protease;Secreted;Signal;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10091328}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..21; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 41,370
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda