| IED ID | IndEnz0002004061 |
| Enzyme Type ID | protease004061 |
| Protein Name |
Probable cytosolic oligopeptidase A EC 3.4.24.70 Thimet metalloendopeptidase 2 Zincin-like metalloproteases family protein 2 |
| Gene Name | CYOP TOP2 At5g10540 F12B17.110 |
| 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 | MASEDTLSSNPLLQNFDFPPFDSVDAHHVRPGIRALLQQLEAELEQLEKAVEPSWPKLVEPLEKIIDRLSVVWGMINHLKAVKDTPELRAAIEEVQPEKVKFQLRLGQSKPIYNAFKAIRESPDWNSLSEARQRLVEAQIKEAVLSGIALEDDKREEFNKIEQELEKLSHKFSENVLDATKKFEKLITDKKEIEGLPPSALGLFAQAAVSKGHETATADTGPWLITLDAPSYLPVMQHAKNRALREEVYRAYLSRASSGDLDNTAIIDQILKLRLEKAKLLGYRNYAEVSMATKMATVEKADELLEKLRSASWDPAVQDIEDLKSFAKNQGAAEADSLTHWDITFWSERLRESKYDINEEELRPYFSLPKVMDALFGLAKTLFGIDVVPADGVAPVWNSDVRFYCVKDSSGNPTAYFYFDPYSRPSEKRDGAWMDEVFSRSRVMAQKGSSVRLPVAQMVCNQTPPVGDKPSLMTFREVETVFHEFGHALQHMLTKEDEGLVAGIRNIEWDAVELPSQFMENWCYHRDTLMSIAKHYQTGETLPENVYKKLLAARTFRAGSLSLRQLKFATVDLELHTKYMPGGAETIYEVDQRVSIKTQVIPPLPEDRFLCSFSHIFAGGYAAGYYSYKWAEVLSADAFSAFEDAGLDDIKAVKETGQRFRNTILALGGGKAPLKVFVEFRGREPSPEPLLRHNGLLAASA |
| Enzyme Length | 701 |
| Uniprot Accession Number | Q949P2 |
| Absorption | |
| Active Site | ACT_SITE 484; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by salicylic acid. {ECO:0000269|PubMed:24004003}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of oligopeptides, with broad specificity. Gly or Ala commonly occur as P1 or P1' residues, but more distant residues are also important, as is shown by the fact that Z-Gly-Pro-Gly-|-Gly-Pro-Ala is cleaved, but not Z-(Gly)(5).; EC=3.4.24.70; |
| DNA Binding | |
| EC Number | 3.4.24.70 |
| Enzyme Function | FUNCTION: Oligopeptidase that may be involved in the degradation of proteasome-generated peptides (By similarity). Binds salicylic acid. {ECO:0000250, ECO:0000269|PubMed:24004003, ECO:0000269|PubMed:24043784}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (11); Chain (1); Coiled coil (1); Erroneous gene model prediction (1); Helix (35); Initiator methionine (1); Metal binding (3); Modified residue (1); Region (1); Turn (11) |
| Keywords | 3D-structure;Acetylation;Coiled coil;Cytoplasm;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | INDUCTION: Up-regulated by pathogen infection, elicitor treatment and flg22, a 22-amino acid sequence of the conserved N-terminal part of flagellin. {ECO:0000269|PubMed:24004003}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:24043784}. |
| Modified Residue | MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0007744|PubMed:22223895 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 4PUT; |
| Mapped Pubmed ID | 12185496; 15028209; 15769804; 16502469; 18433157; 18538804; 27100569; 28627464; 30510037; |
| Motif | |
| Gene Encoded By | |
| Mass | 79,044 |
| Kinetics | |
| Metal Binding | METAL 483; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:24817709, ECO:0007744|PDB:4PUT"; METAL 487; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:24817709, ECO:0007744|PDB:4PUT"; METAL 513; /note="Zinc; catalytic"; /evidence="ECO:0000269|PubMed:24817709, ECO:0007744|PDB:4PUT" |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.70; |