| IED ID | IndEnz0002007838 |
| Enzyme Type ID | protease007838 |
| Protein Name |
Organellar oligopeptidase A, chloroplastic/mitochondrial EC 3.4.24.70 Thimet metalloendopeptidase 1 Zincin-like metalloproteases family protein 1 |
| Gene Name | OOP TOP1 At5g65620 K21L13.14 |
| 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 | MLMATPTSRASLNLLRRSPKPKYFSSSSCHFRPSTFRKSYPCPIWSSSFSFCLPPPRSTTSTSLSSSSFRPFSSPPSMSSAAAAAVESVVSDETLSSNPLLQDFDFPPFDSVDASHVRPGIRALLQHLEAELEELEKSVEPTWPKLVEPLEKIVDRLTVVWGMINHLKAVKDTPELRAAIEDVQPEKVKFQLRLGQSKPIYNAFKAIRESPDWSSLSEARQRLVEAQIKEAVLIGIALDDEKREEFNKIEQELEKLSHKFSENVLDATKKFEKLITDKKEIEGLPPSALGLFAQAAVSKGHENATAENGPWIITLDAPSYLPVMQHAKNRALREEVYRAYLSRASSGDLDNTAIIDQILKLRLEKAKLLGYNNYAEVSMAMKMATVEKAAELLEKLRSASWDAAVQDMEDLKSFAKNQGAAESDSMTHWDTTFWSERLRESKYDINEEELRPYFSLPKVMDGLFSLAKTLFGIDIEPADGLAPVWNNDVRFYRVKDSSGNPIAYFYFDPYSRPSEKRGGAWMDEVVSRSRVMAQKGSSVRLPVAHMVCNQTPPVGDKPSLMTFREVETVFHEFGHALQHMLTKQDEGLVAGIRNIEWDAVELPSQFMENWCYHRDTLMSIAKHYETGETLPEEVYKKLLAARTFRAGSFSLRQLKFASVDLELHTKYVPGGPESIYDVDQRVSVKTQVIPPLPEDRFLCSFSHIFAGGYAAGYYSYKWAEVLSADAFSAFEDAGLDDIKAVKETGQRFRNTILALGGGKAPLKVFVEFRGREPSPEPLLRHNGLLAASASA |
| Enzyme Length | 791 |
| Uniprot Accession Number | Q94AM1 |
| Absorption | |
| Active Site | ACT_SITE 572; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:24043784" |
| 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 degrading short peptides from 8 to 23 amino acid residues. Plays a role in the degradation of transit peptides and of peptides derived from other proteolytic events. Does not exhibit a strict cleavage pattern. Binds salicylic acid. {ECO:0000269|PubMed:24004003, ECO:0000269|PubMed:24043784}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (8); Chain (1); Coiled coil (1); Erroneous initiation (1); Helix (38); Metal binding (3); Mutagenesis (5); Region (1); Transit peptide (1); Turn (12) |
| Keywords | 3D-structure;Chloroplast;Coiled coil;Hydrolase;Metal-binding;Metalloprotease;Mitochondrion;Plastid;Protease;Reference proteome;Transit peptide;Zinc |
| Interact With | |
| Induction | INDUCTION: Not 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: Mitochondrion matrix. Plastid, chloroplast stroma. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 4KA7; 4KA8; |
| Mapped Pubmed ID | 12185496; 16207701; 18431481; 18433157; 18633119; 18775970; 21166475; 24817709; 25910730; 27100569; 27247031; 27837087; 28627464; 30242930; 30510037; 32663165; |
| Motif | |
| Gene Encoded By | |
| Mass | 88,757 |
| Kinetics | |
| Metal Binding | METAL 571; /note=Zinc; catalytic; METAL 575; /note=Zinc; catalytic; METAL 601; /note=Zinc; catalytic |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.70; |