| IED ID | IndEnz0002008049 |
| Enzyme Type ID | protease008049 |
| Protein Name |
Mitochondrial intermediate peptidase MIP EC 3.4.24.59 Octapeptidyl aminopeptidase |
| Gene Name | OCT1 CAGL0D02112g |
| Organism | Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Nakaseomyces Nakaseomyces/Candida clade Candida glabrata (Yeast) (Torulopsis glabrata) Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) |
| Enzyme Sequence | MLIQKILLNKEISRLPRILSILNYTGLRWLSGSSGRNTTELQRIFDDSKYWQSLSENTTQYTKETGLFKNPYLTSTDGLRQFSHDSLHKAHKLAEILRNSVSKEEKVHYIMNLDQLSDTLCRVIDLCEFLRSAHPDQSYVEAAQMCHEEMFEFMNVLNTDVVLCNKLKEVLEDPEILKVLSEEERKVGEILLDDFEKSGIYMKAGIREQFIELSQQISVIGQEFINNTDYVAKEFIKVKRDEMDKSGISPLLTARLNRDLTGKYYKIPTYGQIPLQILKSCPDEDIRKEVWAALHNCPKAQIQRLNQLVRLRVILSNLLGKQSYSDYQLDNKMAGSPENVKGFIKTLMNVTKPLAARELEFIARDKLNAPDSRHMSDNEILSIVKPWDKNYFSSKYDSDNEMAMIRDEQLRYYFSLGNVINGLSELFKRIYGITLQPSRTENGETWSPDVRRLDVISEEEGLVGVIYCDLFERVGKISNPAHFTVCCSRQVYPDENDFTTIQTGQNSDGTVFQLPVISLVCNFSTVALPNGNRTCFLHMNEIETLFHEMGHAMHSMLGRTRLQNISGTRCATDFVELPSILMEHFARDIRVLRTIGSHYETSEPAPEALLNDYLDKTQFLQHCETYSQAKMAMLDQKLHGSFSLSDIERIDSAKIYQKLETRLQVLADDESNWCGRFGHLFGYGATYYSYLFDRAIASKVWDSLFKDDPFNRTGGEKFKERVLKWGGLKNPWSCIADVLEKPDLAKGGAEAMTYIGDSEDL |
| Enzyme Length | 761 |
| Uniprot Accession Number | Q6FW88 |
| Absorption | |
| Active Site | ACT_SITE 548; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal octapeptide as second stage of processing of some proteins imported into the mitochondrion.; EC=3.4.24.59; |
| DNA Binding | |
| EC Number | 3.4.24.59 |
| Enzyme Function | FUNCTION: Cleaves proteins, imported into the mitochondrion, to their mature size. While most mitochondrial precursor proteins are processed to the mature form in one step by mitochondrial processing peptidase (MPP), the sequential cleavage by MIP of an octapeptide after initial processing by MPP is a required step for a subgroup of nuclear-encoded precursor proteins destined for the matrix or the inner membrane (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Metal binding (3); Transit peptide (1) |
| Keywords | Hydrolase;Metal-binding;Metalloprotease;Mitochondrion;Protease;Reference proteome;Transit peptide;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 87,333 |
| Kinetics | |
| Metal Binding | METAL 547; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 551; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 554; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda |