| IED ID | IndEnz0002008054 |
| Enzyme Type ID | protease008054 |
| Protein Name |
Mitochondrial intermediate peptidase MIP EC 3.4.24.59 Octapeptidyl aminopeptidase |
| Gene Name | OCT1 UMAG_02435 |
| Organism | Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Ustilaginomycotina Ustilaginomycetes Ustilaginales Ustilaginaceae Ustilago Ustilago maydis (Corn smut fungus) Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus) |
| Enzyme Sequence | MASTSKNAQRAAASVAHSYHVCLARRMSRLPTLLSNISAPAASKALDRYESKRIHSRSFSSSLAAQRVQRPTSAGPILTNPISDHEKDNDELRSLFDAPPTSSSANHLRSSGPSTGLFEIPSLTSPQNFLVLAQQTLARAQLLVDRIDRAGSADASTAQGIKELKEVVRNLDRLSDLLCGVIDMAELVRNAHPDPEWAEAANAAYEYLCGYMNVLNTHTGLYSVLKNILSIKEVAETLSKEATAVAQVFLRDFEKSGIHLPPAERERFVQLSDEILVLGRGFLQDIAGNDASDDFARIASAQADADKSDMVGLPTHWLEDVNPTILKAVRASAITDTDGLLTFSAADQPWVFQTLLKYAPDERARKVAFRAANYGSQAQVQRLERLLKARAELATLTGASSYAEMALGDKMAKEPQNVEEFLRALTKHHRPRASHDLDKLRRLKHNATVSEPAQNTRQSTFNTNSTLPEFAPWDRDMYTEQHFRSASLSNVQPLSPYLSVGSVFAGLSRLFSALYGIRFRASMVAPGEVWSEGAGDVMKVEVLDESEGARGTSGSAEGLIGTIYADLWSREGKPGGAAHYTVRCSRRVDKDDEAGDFTYGRAEDGRVVRPQDLGGEGCGNPLQAPTFEQRERPGRYQLPVVVLMCDFARPGNANQGPCLLGWHEVETLFHEMGHAIHSMIGRTSYHNVSGTRCATDFVELPSILMEHFVSSPQVVHLLARHHSTGASLPFEHLSSHLAASKSLEGLDTYHQILLARLDQLYHSQLAASPSFSSTTTYSDLDRQMHLPGAPNLSYTEGAHPQVRFGHLFGYGSTYYSYLLDRVIASKVWNHLFANNPLDRYAGQVFKNQCLKYGGGKDPWHILADVLNEDSVRQGDSRAMQQVGKWGIEC |
| Enzyme Length | 889 |
| Uniprot Accession Number | Q4PBS8 |
| Absorption | |
| Active Site | ACT_SITE 671; /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); Compositional bias (2); Metal binding (3); Region (1); 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 | 97,799 |
| Kinetics | |
| Metal Binding | METAL 670; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 674; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 677; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda |