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 |