| IED ID | IndEnz0002006362 |
| Enzyme Type ID | protease006362 |
| Protein Name |
Mitochondrial presequence protease EC 3.4.24.- |
| Gene Name | CYM1 CAGL0F03157g |
| 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 | MLRFQRFASTYNQRAVLRKYPVGGIIHGFQVRRAVPVPELKLTAVDLIHEQTGAEHLHIDRDDKNNVFSIAFRTLPPDATGVPHILEHTTLCGSEKYPVRDPFFKMLNKSLANFMNAMTGPDYTFFPFATTNARDFVNLRDVYLNSTLRPLLKEQDFYQEGWRLEHSEVTNPKSDIIFKGVVFNEMKGQVSNADYHFWSQFQQNIYPSLNNSGGDPQKITDLHYQDLVDFHHANYHPSNARTFTYGSFPLEDTLKKVNEEFRAYGKRIINKKLPKPLELIETKELTLEGQIDPMLPAEKQTKTSLTWKCGEPTDLYETFLLKILGNLLLDGHDSIMYKGLIESGLGHDFSVNTGVESMTAANFLTVGIQGSQNVEEFKSKVFDLFKEFIENDVDSNKVDAIIHQLELSKKDQKADFGLQILYSILPGWTNGIDPIEGLEFDELIGRLKSDFKENGTKIFKNILDKYIIDQPYFHFTMKGSEEFSSKLAAEESTKLDKKLKELDETDRKAIFERGLLLEAAQNHKEDLSCLPTLGVADISRKVDTYDLNTNANITVRNTATNGISYIRGKKLINDMIPLELYPFLSLFAASLTHLGTKTTPYGAIDNEIKLHTGGISTNISVNADPTTLQPNLYFDMSGFSLNEKSDYIFNFLKTILMETDFSTHKDKLKVLINSIASSNTSHIADSGHTVARSFASGHLSTVAAIQEHISGVEHYKLISRLCSIMNDDKLFQSEVIDKLVMLQRIIVNSQNMEFFASVDCQAQENKIRKEVDYFVSTLPNTSSDISGAIQTACVPRYSDSQVLNLIKFPFQVHYTAQAYNGVSYTHKDGAALQVLANMLTFKHLHKEIREKGGAYGGGATFSALSGIFSYYSYRDPNPLASIQTFEKSASYVLNDAKWTQSDLDESKLSIFQQVDAPISPKSEGSTFFNLGVTDEMRQVRREQLLDTSLLDIHRVAERYILPNKSIATVVGPGIDGETVSPKWHIEDIKV |
| Enzyme Length | 990 |
| Uniprot Accession Number | Q6FUI7 |
| Absorption | |
| Active Site | ACT_SITE 87; /note=Proton acceptor; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: ATP-independent protease that degrades mitochondrial transit peptides after their cleavage. Also degrades other unstructured peptides (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Metal binding (3) |
| Keywords | Hydrolase;Metal-binding;Metalloprotease;Mitochondrion;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 111,695 |
| Kinetics | |
| Metal Binding | METAL 84; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 88; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 185; /note=Zinc; catalytic; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |