IED ID | IndEnz0002014279 |
Enzyme Type ID | protease014279 |
Protein Name |
Glyoxysomal processing protease, glyoxysomal AtDEG15 EC 3.4.21.- DEG-protease |
Gene Name | DEG15 GPP At1g28320 F3H9.2 F3H9.3 |
Organism | Arabidopsis thaliana (Mouse-ear cress) |
Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress) |
Enzyme Sequence | MDVSKVVSFSRNFAVLVKVEGPDPKGLKMRKHAFHQYHSGNATLSASGILLPRDIFLSGEVAAKVLFEAGQDMALVLTVASVVEPFLTLGHRTSSSISQDPVKLIPGAMIEIMVEGQLKSEKEAPFWVPAQLLSLVDVPVSSAALQSLIEASSGSKDSGWDIGWSLVSAANGSQPSINIEHYSKPLMQLDEPHNANFMAKSATRMAILGVPLSLLGQPSMNFASSSSKGDTLVALGSPFGILSPVNFFNSVSTGSIANSYPSGSLKKSLMIADVRCLPGMEGAPVFAKNGHLIGILIRPLRQKNSGVEIQLVVPWGAITTACSHLLLEEPSVEGKASQWGSEVLSVKSDASIPAQVAIEKAMESVCLITVNDGVWASGIILNEHGLILTNAHLLEPWRYGKGGVYGEGFKPYVLGAEEFSSTGSKFWEQKSQTLPRKAPRNHYSSVGENIREYKHNFLQTGHRDIRVRLCHLDSWTWCPANVVYICKEQLDIALLQLEYVPGKLQPITANFSSPPLGTTAHVVGHGLFGPRCGLSPSICSGVVAKVVHAKRRLNTQSISQEVAEFPAMLETTAAVHPGGSGGAVLNSSGHMIGLVTSNARHGAGTVIPHLNFSIPCAVLAPIFKFAEDMQNTTILQTLDQPSEELSSIWALMPSLSPKTEQSLPNLPKLLKDGNNKQTKGSQFAKFIAETQDMFVKPTKLSRDVIPSKL |
Enzyme Length | 709 |
Uniprot Accession Number | Q8VZD4 |
Absorption | |
Active Site | ACT_SITE 392; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 491; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 580; /note=Charge relay system; /evidence=ECO:0000250 |
Activity Regulation | ACTIVITY REGULATION: Inhibited by N-methylmaleimide (NEM), but not by E64, benzamidine, aprotinin, leupeptin, pefabloc, pepstatin A, EGTA, EDTA and 1,10-phenanthroline. {ECO:0000269|PubMed:18952862}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.21.- |
Enzyme Function | FUNCTION: Trypsin-like serine endopeptidase involved in the processing of glyoxysomal higher molecular weight precursor. The dimeric form carries out the specific cleavages needed to remove PTS2-containing presequences, whereas the monomeric form degrades the removed presequences and misfolded proteins (Probable). Not required for degradation of glyoxylate cycle enzymes during seedling development. {ECO:0000269|PubMed:17592111, ECO:0000269|PubMed:18952862, ECO:0000269|PubMed:19748917, ECO:0000305}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1); Erroneous gene model prediction (1); Mutagenesis (11); Sequence conflict (1) |
Keywords | Hydrolase;Peroxisome;Protease;Reference proteome;Serine protease |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:15333753, ECO:0000269|PubMed:18952862}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 17181860; 18775970; 22008015; 22520048; 23943091; 31236542; |
Motif | |
Gene Encoded By | |
Mass | 76,126 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |