| IED ID | IndEnz0002015452 |
| Enzyme Type ID | protease015452 |
| Protein Name |
Lon protease homolog, mitochondrial EC 3.4.21.53 |
| Gene Name | PIM1 YALI0F26169g |
| Organism | Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Dipodascaceae Yarrowia Yarrowia lipolytica (Candida lipolytica) Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica) |
| Enzyme Sequence | MIDNKVSVCSVGKVVITEVATFASHPLYIDRKTALTMIRSTRAASRLRLGARYYASHAPYGVLSEHLKRTPRTNSQHYYPPPQGAHDLPKVSSMGDSIASIVRGRELWVQEKDKSDKPEKSDKPDKTDKTDKDKPEKQDKDKTDKPEKTKVSHTPSSTASTGAGEAAAPPSAPPSGSGSSSSSGGGSPPAKKKKSPAQTYPEILAVPISDRPLLPGFHRALVIRDPNVMKAIDEMITRGEPYLACFFLKEFSNADVIQDASEVHDIGVIAEIQIQSQDHKRSTVDASNEPVYVLILYPHKRVRLNSLKNPPSSGGAVSYASVSEDVAEDGELLLTSKDLEGYSEEFLEAREEAKKAKSGKTEDSKHDSKVTSKDGKETTEKYDSSTLQESPYSFLSTYDVSTAAISLIEDKPHDKNNRVITTLTNEILNVFKMLRAEDATLREQLSSVVGDILRTEPAVLQEPGRLADFAAALCAGEGKEIQAVLTALDLETRLNRALILLKREHTNAKLQQKIARDVENKLNSKHKKFLLTEQMKAIKKELGVDDGKEKLVEKFNERAEKLDMPENIQKVFEEEMTRLQSMEPSSSEYSVTRNYLDWITQIPWNKTTEDRFNLPQAKDVLDSEHYGMKEVKDRILEFIAVSRMKGGLTGKILLLQGPPGVGKTSIGKSIAKALNRQFYRFSVGGTNDASEVKGHRRTYVGAIPGRLVQALKQTQTENPLILIDEIDKLSSSRTQGDPGAALLEALDPEQNNAFLDHYLDVPIDLSKVLFVCTSNDLSTIPWPLLDRMEVIEMSGYVPDEKLNIANQYLVPQSKKETGLENVNVQVTDDAINALNRQYCRESGVRNLKKHIEKIFRKVVVKIVGEYGQDEVAAEKIIDVEPVEKDKESAEKKTTKSKSKEVNEEPAAKEEKDKATESAESSETKVGTKAPPVTVPEDYSLTIDEKDLYDYVNSPPYSSDRMFEDPPPGVVMGLAYSPLGGSALYIECILDGGLSADSSARLSSTGNLGNVMKESTNIAYSFAKSFMIRNFPANRFFERAGIHLHCPAGAISKDGPSAGCAVVTGLLSLALNHPIDSSISMTGEISLTGKVMKIGGLREKAVGAHSAGAKTIIIPKDNSGDWDELPDTVKEGLTPVFAGTYQDVYDVVFQGLDTKVAAEVWKKQFDLIDRKLDKRGSK |
| Enzyme Length | 1177 |
| Uniprot Accession Number | Q6C0B5 |
| Absorption | |
| Active Site | ACT_SITE 1056; /evidence=ECO:0000255|HAMAP-Rule:MF_03120; ACT_SITE 1099; /evidence=ECO:0000255|HAMAP-Rule:MF_03120 |
| 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_03120}; |
| DNA Binding | |
| EC Number | 3.4.21.53 |
| Enzyme Function | FUNCTION: ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner. {ECO:0000255|HAMAP-Rule:MF_03120}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 657..664; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_03120 |
| Features | Active site (2); Chain (1); Compositional bias (4); Domain (2); Nucleotide binding (1); Region (3) |
| Keywords | ATP-binding;DNA-binding;Hydrolase;Mitochondrion;Nucleotide-binding;Protease;Reference proteome;Serine protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03120}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 129,478 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |