| IED ID | IndEnz0002002927 |
| Enzyme Type ID | protease002927 |
| Protein Name |
Lon protease homolog, mitochondrial EC 3.4.21.53 |
| Gene Name | PIM1 CAGL0J04422g |
| Organism | Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Nakaseomyces Nakaseomyces/Candida clade Candida glabrata (Yeast) (Torulopsis glabrata) Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) |
| Enzyme Sequence | MLGTRVTRAVYTRAPLKLQLRALGLHRRYVHNGSKNDEGSSTSTTTNKEENDKKLPDVYPQMLALPISRRPLFPGFYKAVVISEPRVMKAITDMVERQQPYIGAFMLKDSNNDTDIIHDISEVHELGVLAQVTSAFPSKDEKTGKETMTALLYPHKRIKIDQLIPPKDVKIEDIVVEKVVDNEVASEETKDEETVDKTESATDKVSEEITEEIAKAPSTEVTEDPDNYENPTDFLKDYNVTLVNVSNLEDEPFDIKSPIINALTSEILKVFKEISQLNSMFREQIATFSASIQSATTNIFEEPAKLADFAAAVSAGEEEELQEVLESLNIEQRLEKSLLVLKKELMNAELQNKISKDVETKIQKRQKEYYLMEQLKGIKRELGIDDGRDKLVDTYKKRVEKLNLPENVQKTFDEEITKLATLETSMSEFGVIRNYLDWLTSLPWGINSKEQYSIPRARKILDEDHYGMKDVKDRILEFIAVGKLLGKVDGKIICFVGPPGVGKTSIGKSISRALNRQFFRFSVGGMTDVAEIKGHRRTYIGALPGRIIQALKKCQTQNPLILIDEIDKIGHGGIHGDPSAALLEVLDPEQNNSFLDNYLDIPIDLSKVLFVCTANSLDTIPRPLLDRMEVIELTGYVAEDKIKIAEQYLVPSAKKTAGLQNATVSMDEEAINALMKYYCRESGVRNLKKHIEKIYRKAALEVVKKMSIEDTEPLVSTSEEPQLSQTNQNISSSSAEDSTTDLEDSVNPDTAKEASKPNNSQEGASVEETKKAVKTEEEEDTSMIVPEDIKVEITPEDLKKYVGPPIYTTDRLYETTPPGVIMGLAWTNMGGCSLYVESVLEQPLHNCKHANLERTGQLGDVMKESSRLAYSFSKMYLSKKFPENRFFEKAAIHLHCPEGATPKDGPSAGVTMATSFLSLALNKPVDPTVAMTGELTLTGKVLRIGGLREKVVAAKRSGAKTVIFPKDNLNDWEELPENVKEGMEPLAADWYDDIYKRLFSGVKKSEGNNVWKSEFELIDKKKKEND |
| Enzyme Length | 1026 |
| Uniprot Accession Number | Q6FPE6 |
| Absorption | |
| Active Site | ACT_SITE 907; /evidence=ECO:0000255|HAMAP-Rule:MF_03120; ACT_SITE 950; /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 497..504; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_03120 |
| Features | Active site (2); Chain (1); Compositional bias (2); Domain (2); Nucleotide binding (1); Region (3); Transit peptide (1) |
| Keywords | ATP-binding;DNA-binding;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}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 114,998 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |