Detail Information for IndEnz0002014279
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