| IED ID | IndEnz0002015719 |
| Enzyme Type ID | protease015719 |
| Protein Name |
Intermediate cleaving peptidase 55 EC 3.4.11.26 Intermediate cleaving peptidase of 55 kDa |
| Gene Name | ICP55 YER078C |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MLHRINPVRFSMQSCQRYFSKLVSPLEQHKSNTFTNRVRIPIEAGQPLHETRPFLIKSGELTPGISALEYYERRIRLAETLPPKSCVILAGNDIQFASGAVFYPFQQENDLFYLSGWNEPNSVMILEKPTDSLSDTIFHMLVPPKDAFAEKWEGFRSGVYGVQEIFNADESASINDLSKYLPKIINRNDFIYFDMLSTSNPSSSNFKHIKSLLDGSGNSNRSLNSIANKTIKPISKRIAEFRKIKSPQELRIMRRAGQISGRSFNQAFAKRFRNERTLDSFLHYKFISGGCDKDAYIPVVATGSNSLCIHYTRNDDVMFDDEMVLVDAAGSLGGYCADISRTWPNSGKFTDAQRDLYEAVLNVQRDCIKLCKASNNYSLHDIHEKSITLMKQELKNLGIDKVSGWNVEKLYPHYIGHNLGLDVHDVPKVSRYEPLKVGQVITIEPGLYIPNEESFPSYFRNVGIRIEDDIAIGEDTYTNLTVEAVKEIDDLENVMQNGLSTKFEEDQVAPL |
| Enzyme Length | 511 |
| Uniprot Accession Number | P40051 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=The enzyme cleaves the 36-Pro-Pro-37 bond of cysteine desulfurase (EC 2.8.1.7) removing three amino acid residues (Tyr-Ser-Pro) from the N-terminus after cleavage by mitochondrial processing peptidase.; EC=3.4.11.26; Evidence={ECO:0000269|PubMed:19720832, ECO:0000269|PubMed:19837041}; |
| DNA Binding | |
| EC Number | 3.4.11.26 |
| Enzyme Function | FUNCTION: Aminopeptidase which cleaves preprotein intermediates that carry destabilizing N-ter amino acid residues after the mitochondrial processing peptidase (MPP) cleavage site and is thus critical for stabilization of the mitochondrial proteome. {ECO:0000269|PubMed:19720832, ECO:0000269|PubMed:19837041}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (17); Chain (1); Helix (17); Metal binding (7); Turn (2) |
| Keywords | 3D-structure;Aminopeptidase;Hydrolase;Manganese;Membrane;Metal-binding;Metalloprotease;Mitochondrion;Mitochondrion inner membrane;Nucleus;Protease;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19720832}. Mitochondrion inner membrane {ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:19720832}; Peripheral membrane protein {ECO:0000269|PubMed:19720832}; Matrix side {ECO:0000269|PubMed:19720832}. Note=Has the same dual localization (mitochondrion and nucleus) as one of its substrate, NFS1. {ECO:0000269|PubMed:19720832}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 6A9T; 6A9U; 6A9V; |
| Mapped Pubmed ID | 11283351; 11805837; 15772085; 16554755; 19536198; 20489023; 21525245; 21929734; 22172993; 23212899; 23479443; 23964590; 24116217; 24943357; 25435547; 30582634; |
| Motif | |
| Gene Encoded By | |
| Mass | 57,990 |
| Kinetics | |
| Metal Binding | METAL 327; /note=Manganese 2; /evidence=ECO:0000255; METAL 338; /note=Manganese 1; /evidence=ECO:0000255; METAL 338; /note=Manganese 2; /evidence=ECO:0000255; METAL 417; /note=Manganese 1; /evidence=ECO:0000255; METAL 444; /note=Manganese 1; /evidence=ECO:0000255; METAL 467; /note=Manganese 1; /evidence=ECO:0000255; METAL 467; /note=Manganese 2; /evidence=ECO:0000255 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.26;3.4.11.9; |