IED ID | IndEnz0002015623 |
Enzyme Type ID | protease015623 |
Protein Name |
Lon protease homolog 2, peroxisomal EC 3.4.21.53 |
Gene Name | PICST_45980 |
Organism | Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545) (Yeast) (Pichia stipitis) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Debaryomycetaceae Scheffersomyces Scheffersomyces stipitis (Yeast) (Pichia stipitis) Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545) (Yeast) (Pichia stipitis) |
Enzyme Sequence | MARYKNPKSPAKLKQQIVLPTCKLDSNLVLLPGIIYNVTFSRFKAAALLYRYKDLVSQVSIINNLLNEYEFNPSKDSDSVEEDDMVTSPITISKVAVEGIEQFFKYEAAFKNSQGLVSEKDIAEVAPSNEFDWLTLAIKPNLEKIKEPSNAQIDPTEHNSVVTIARIVGIVDDTTNIKLTLQAITRGLKIAPKKKTRPNEQLLEVDWSSDIPELRRHFKSLKDSSLDLFKVIDKFIVDYRQALSINSANGNKSNLQITKPGSRYKGANGSSQKPGDLLTLNPLANALYLQLAGSKDFSKAFLSLQKLYGQFASDENLKVDTKSYLRLLDLTCGILPFPNHEKLKLLHKISIDDRGNELINMINQLIKIFDTLDGNNSFVNHWFYNEATNIQKANVVANQLKSIRLLLEGMTNKTRPISNRGNIKSFNNSENGNNNKTNGSGITSRRPKSNEDGGEVYDEEDDDEEDDELRAITNFIKYKLPNITTLSPDSKRLIIKDFKRIRASSQSPGGGGNSDFHVIRNYLEIVMDIPWDKYVTKFKSNKDIDLNFAKKQLDDDHYGLEHVKKRLIQYLVVLKLLGINAEKQISDFRKENQVPSPSSSGSNLATQNSLVPASSIVIANNDETSFAHKQAQNKVKTSIKESNIENQTNQSIQVTKYNKSPIIMLAGPPGTGKTSLAKSIASSLGRNFQRISLGGVKDESEIRGHRRTYVGAMPGLIIQALRKSRSMNPVILLDEIDKVIGGSSGVNKFNGDPSAALLEVLDPEQNTSFIDHYLGFPVDLSQVIFICTANEPHNLTRPLLDRLEMIEVSAYDYNEKLIIGRKYLLPRQVKRNGFPASDRIEEFVNIDDASMKKIIVDYTREAGVRNLERKLGTICRFKAVEYCEGLSGKSFYNPNVEEADLPKYLGIPYSSGDFSSIETTISNNSRVGIVNGLSYNSDGSGSVLVFETIGFDKRVGNPNSSNTGCSLVMTGRLGEVLMESGKIGLTFIKSLIYKNLIQAKEQPDDKYLIEKFNNLELNLHVPMGSISKDGPSAGITMATSFLSVILDKPVPADVAMTGEITLRGLVLPIGGVKEKMMGAHLNGNIRRMIVPRENRKDLIEEFSRSVEEAGDVVDSNLMNELLKDNEEADFKMDKVEKFYLKRYGIQIFYAREFYDVMKILWGEDDLLTKPKSNRILEYHL |
Enzyme Length | 1180 |
Uniprot Accession Number | A3LUF7 |
Absorption | |
Active Site | ACT_SITE 1032; /evidence=ECO:0000255|HAMAP-Rule:MF_03121; ACT_SITE 1075; /evidence=ECO:0000255|HAMAP-Rule:MF_03121 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53; Evidence={ECO:0000255|HAMAP-Rule:MF_03121}; |
DNA Binding | |
EC Number | 3.4.21.53 |
Enzyme Function | FUNCTION: ATP-dependent serine protease that mediates the selective degradation of misfolded and unassembled polypeptides in the peroxisomal matrix. Necessary for type 2 peroxisome targeting signal (PTS2)-containing protein processing and facilitates peroxisome matrix protein import. {ECO:0000255|HAMAP-Rule:MF_03121}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | NP_BIND 667..674; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_03121 |
Features | Active site (2); Chain (1); Compositional bias (1); Domain (2); Nucleotide binding (1); Region (1) |
Keywords | ATP-binding;Hydrolase;Nucleotide-binding;Peroxisome;Protease;Reference proteome;Serine protease |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000255|HAMAP-Rule:MF_03121}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 132,053 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |