| IED ID | IndEnz0002006575 |
| Enzyme Type ID | protease006575 |
| Protein Name |
Lon protease homolog, mitochondrial EC 3.4.21.53 |
| Gene Name | PIM1 LON YBL022C YBL0440 |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MLRTRTTKTLSTVARTTRAIQYYRSIAKTAAVSQRRFASTLTVRDVENIKPSHIIKSPTWQEFQHQLKDPRYMEHFAQLDAQFARHFMATNSGKSILAKDDSTSQKKDEDVKIVPDEKDTDNDVEPTRDDEIVNKDQEGEASKNSRSSASGGGQSSSSRSDSGDGSSKQKPPKDVPEVYPQMLALPIARRPLFPGFYKAVVISDERVMKAIKEMLDRQQPYIGAFMLKNSEEDTDVITDKNDVYDVGVLAQITSAFPSKDEKTGTETMTALLYPHRRIKIDELFPPNEEKEKSKEQAKDTDTETTVVEDANNPEDQESTSPATPKLEDIVVERIPDSELQHHKRVEATEEESEELDDIQEGEDINPTEFLKNYNVSLVNVLNLEDEPFDRKSPVINALTSEILKVFKEISQLNTMFREQIATFSASIQSATTNIFEEPARLADFAAAVSAGEEDELQDILSSLNIEHRLEKSLLVLKKELMNAELQNKISKDVETKIQKRQREYYLMEQLKGIKRELGIDDGRDKLIDTYKERIKSLKLPDSVQKIFDDEITKLSTLETSMSEFGVIRNYLDWLTSIPWGKHSKEQYSIPRAKKILDEDHYGMVDVKDRILEFIAVGKLLGKVDGKIICFVGPPGVGKTSIGKSIARALNRKFFRFSVGGMTDVAEIKGHRRTYIGALPGRVVQALKKCQTQNPLILIDEIDKIGHGGIHGDPSAALLEVLDPEQNNSFLDNYLDIPIDLSKVLFVCTANSLETIPRPLLDRMEVIELTGYVAEDKVKIAEQYLVPSAKKSAGLENSHVDMTEDAITALMKYYCRESGVRNLKKHIEKIYRKAALQVVKKLSIEDSPTSSADSKPKESVSSEEKAENNAKSSSEKTKDNNSEKTSDDIEALKTSEKINVSISQKNLKDYVGPPVYTTDRLYETTPPGVVMGLAWTNMGGCSLYVESVLEQPLHNCKHPTFERTGQLGDVMKESSRLAYSFAKMYLAQKFPENRFFEKASIHLHCPEGATPKDGPSAGVTMATSFLSLALNKSIDPTVAMTGELTLTGKVLRIGGLREKAVAAKRSGAKTIIFPKDNLNDWEELPDNVKEGLEPLAADWYNDIFQKLFKDVNTKEGNSVWKAEFEILDAKKEKD |
| Enzyme Length | 1133 |
| Uniprot Accession Number | P36775 |
| Absorption | |
| Active Site | ACT_SITE 1015; /evidence=ECO:0000255|HAMAP-Rule:MF_03120; ACT_SITE 1058; /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 (PubMed:15870080, PubMed:16428434, PubMed:8146662, PubMed:8276800, PubMed:8354406, PubMed:8810243, PubMed:9405361, PubMed:9724747). Endogenous substrates include ABF2, ACO2, ILV1, ILV2, LSC1, LYS4, MGM101 and several oxidized proteins. The 2 nucleic acid-binding proteins ABF2 and MGM101 are protected from degradation by PIM1 when they are bound to DNA (PubMed:16428434, PubMed:20150421, PubMed:28377575). {ECO:0000255|HAMAP-Rule:MF_03120, ECO:0000269|PubMed:15870080, ECO:0000269|PubMed:16428434, ECO:0000269|PubMed:20150421, ECO:0000269|PubMed:28377575, ECO:0000269|PubMed:8146662, ECO:0000269|PubMed:8276800, ECO:0000269|PubMed:8354406, ECO:0000269|PubMed:8810243, ECO:0000269|PubMed:9405361, ECO:0000269|PubMed:9724747}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.9. {ECO:0000269|PubMed:8354406}; |
| Pathway | |
| nucleotide Binding | NP_BIND 632..639; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_03120 |
| Features | Active site (2); Chain (1); Compositional bias (6); Domain (2); Mutagenesis (2); Nucleotide binding (1); Propeptide (1); Region (3); Sequence conflict (1); Transit peptide (1) |
| Keywords | ATP-binding;DNA-binding;Direct protein sequencing;Hydrolase;Mitochondrion;Nucleotide-binding;Protease;Reference proteome;Serine protease;Transit peptide |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03120, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:9405361}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10906275; 11212342; 11805826; 11805837; 12381727; 12657466; 14729968; 16336126; 16429126; 18359303; 19536198; 19538506; 20186747; 21209324; 21936842; 22119779; 22663076; 22688810; 23202731; 23212899; 23220263; 23479443; 23932848; 24024159; 24040173; 27246605; 27387767; 27693354; 7957078; 8592469; 8636205; 8988248; 9106654; 9149530; 9585511; |
| Motif | |
| Gene Encoded By | |
| Mass | 127,112 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=40 uM for ATP for ATPase activity {ECO:0000269|PubMed:8354406}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.53; |