| IED ID | IndEnz0002004558 |
| Enzyme Type ID | protease004558 |
| Protein Name |
Lon protease homolog 2, peroxisomal EC 3.4.21.53 |
| Gene Name | PLN |
| Organism | Pichia angusta (Yeast) (Hansenula polymorpha) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Pichiaceae Ogataea Pichia angusta (Yeast) (Hansenula polymorpha) |
| Enzyme Sequence | MSSKSSAWQVELPVHRLERNLIFLPGITYRVVFDKQKALDLASRWSAKERSERVAAIASRFGLSSKHLVACVPGYPDSDTCTVCVVNGFYEMSETTVVSFKGVTRGYIVQSDEDTATVEIQEETSVPHPDTKDMIRLFDNIDQFLTYYKDEGTLDSEDKEERSRHILLRLTPLATLLNAQLSASDVSAGLKRLRQAYGRKSGDFAHYNDVLVALFPFPIELKISYLRSKGAERIEVFNKCVAFANKVFEEHLDTSYLAEIWSSLDHHSSKAQSNVSRSQFISNHLRNLRRLVEEMGLMRVTGRGSRTAEDNDENKSIQDFVDSLDKYLINEDGKRLIAKDFERLKQMQSSSSDYQVLRAYLEIIMDLPWQRLDSFVESVNVDLARAREQLDADHYGMESAKERILEYLAVLNLHNQKQPRHEPEFVYGTGDEPTTKERPASTLKAPILLLTGPPGVGKTSLARSIATTLGRKFQRISVGGLNDFADLKGHRRTYVGAIPGLIVQALRRSQSMNPVILLDEVDKIGSNSRKGDPEAALLEILDPEQNTNFHDHYIGFPIDLSQILFVCTSNDLWQLSDPLRDRMEVIELAGYNYMEKVEISKKYLIPRQLERAGLSSDAVAMDDETILKMATHYTSEPGIRNLERLIAAICRGKAVERQMGEATKTVTVHDLAKYIGSPSHLRATAAGETKFQKGYGVVNGLSYNSDGSGSLLRFEMIGLPGSQKMNCTGRLGEVLLESSQIANTLVGYLLHNNLVAGTQEFRDELLKRYENTSVHLHVPEGAISKDGPSAGITMTLCLMSLVLRKKVPETLAMTGEITLTGKVLPIGGVREKLLGAHLAGKVNKVLLPRQNRKDVIEDFIYNLRNRELAKELFAKFLDEEEQLLKEGRTHAGEPEKWVYQTLGLEIVYVDDFSDVLASVWEGEVLLTGGIREARI |
| Enzyme Length | 935 |
| Uniprot Accession Number | Q2V573 |
| Absorption | |
| Active Site | ACT_SITE 789; /evidence=ECO:0000255|HAMAP-Rule:MF_03121; ACT_SITE 832; /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, ECO:0000269|PubMed:17172804}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 452..459; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_03121 |
| Features | Active site (2); Chain (1); Domain (2); Motif (1); Nucleotide binding (1) |
| Keywords | ATP-binding;Hydrolase;Nucleotide-binding;Peroxisome;Protease;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 | MOTIF 933..935; /note=Microbody targeting signal; /evidence=ECO:0000255|HAMAP-Rule:MF_03121 |
| Gene Encoded By | |
| Mass | 104,880 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.6.4.7; |