Detail Information for IndEnz0002015623
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