Detail Information for IndEnz0002014370
IED ID IndEnz0002014370
Enzyme Type ID protease014370
Protein Name Phytepsin
EC 3.4.23.40
Aspartic proteinase

Cleaved into: Phytepsin 32 kDa subunit; Phytepsin 29 kDa subunit; Phytepsin 16 kDa subunit; Phytepsin 11 kDa subunit
Gene Name
Organism Hordeum vulgare (Barley)
Taxonomic Lineage cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae Liliopsida Petrosaviidae commelinids Poales Poaceae BOP clade Pooideae Triticodae Triticeae Hordeinae Hordeum Hordeum vulgare (Barley)
Enzyme Sequence MGTRGLALALLAAVLLLQTVLPAASEAEGLVRIALKKRPIDRNSRVATGLSGGEEQPLLSGANPLRSEEEGDIVALKNYMNAQYFGEIGVGTPPQKFTVIFDTGSSNLWVPSAKCYFSIACYLHSRYKAGASSTYKKNGKPAAIQYGTGSIAGYFSEDSVTVGDLVVKDQEFIEATKEPGITFLVAKFDGILGLGFKEISVGKAVPVWYKMIEQGLVSDPVFSFWLNRHVDEGEGGEIIFGGMDPKHYVGEHTYVPVTQKGYWQFDMGDVLVGGKSTGFCAGGCAAIADSGTSLLAGPTAIITEINEKIGAAGVVSQECKTIVSQYGQQILDLLLAETQPKKICSQVGLCTFDGTRGVSAGIRSVVDDEPVKSNGLRADPMCSACEMAVVWMQNQLAQNKTQDLILDYVNQLCNRLPSPMGESAVDCGSLGSMPDIEFTIGGKKFALKPEEYILKVGEGAAAQCISGFTAMDIPPPRGPLWILGDVFMGPYHTVFDYGKLRIGFAKAA
Enzyme Length 508
Uniprot Accession Number P42210
Absorption
Active Site ACT_SITE 102; ACT_SITE 289
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Prefers hydrophobic residues Phe, Val, Ile, Leu, and Ala at P1 and P1', but also cleaves -Phe-|-Asp- and -Asp-|-Asp- bonds in 2S albumin from plant seeds.; EC=3.4.23.40;
DNA Binding
EC Number 3.4.23.40
Enzyme Function FUNCTION: Involved in the breakdown of propeptides of storage proteins in protein-storage vacuoles. {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Beta strand (23); Chain (4); Disulfide bond (6); Domain (2); Glycosylation (1); Helix (19); Propeptide (1); Signal peptide (1); Site (2); Turn (4)
Keywords 3D-structure;Aspartyl protease;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Protease;Signal;Vacuole;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:8653791}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..27; /evidence=ECO:0000255
Structure 3D X-ray crystallography (1)
Cross Reference PDB 1QDM;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 54,226
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda