| IED ID | IndEnz0005001235 |
| Enzyme Type ID | lipase001235 |
| Protein Name |
Probable cardiolipin-specific deacylase 1, mitochondrial EC 3.5.1.- |
| Gene Name | SPAC6G10.03c |
| Organism | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota Taphrinomycotina Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces Schizosaccharomyces pombe (Fission yeast) Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
| Enzyme Sequence | MSQVKVAVRSEEAANSYTQTFGMSWRQWRQACSEEYAKQCEREVLHTVDFIRENEKDPERLVEVVDSKIYDNDGLVHEVCVSDKATGKANKRSIVYMHGYGAGLGFYFRNMDGLTKGVTKDFNSYFVDWLGMGNSSRPPFDIKGQTASEKVEETERFFTESLETWRIGHGIEKMILVGHSMGGYLSAVYAMQYPERVEKLLLVSPVAIPENPFASNDDAEVYNSVASSAVHAVMDEPPLSNVTNEVLQTQEETTGLEPSRPSKPKNPLPRFITFLWEQNVTPFSLLRLSGPLGPKLMSFWSSRRFSTLPPETFRALHNYCYSIFRLKGSSEYALGNLLAPGAFARRCIMNRLRMLKCRTIFMYGDKDWMDDVAGLEATNRLKEMNIEAEHHIISNAGHHCYLDNPEDFNEIVLKEIRMSLRSFSSISE |
| Enzyme Length | 428 |
| Uniprot Accession Number | O14249 |
| Absorption | |
| Active Site | ACT_SITE 180; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P53264; ACT_SITE 367; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P53264; ACT_SITE 398; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P53264 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a cardiolipin + H2O = 1'-[1,2-diacyl-sn-glycero-3-phospho],3'-[1-acyl-sn-glycero-3-phospho]-glycerol + a fatty acid + H(+); Xref=Rhea:RHEA:32935, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:62237, ChEBI:CHEBI:64743; Evidence={ECO:0000250|UniProtKB:P53264};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32936; Evidence={ECO:0000250|UniProtKB:P53264}; |
| DNA Binding | |
| EC Number | 3.5.1.- |
| Enzyme Function | FUNCTION: Mitochondrial cardiolipin-specific phospholipase which deacylates de novo synthesized cardiolipin (CL). Part of the remodeling process of cardiolipin, which involves deacylation-reacylation of premature cardiolipin. {ECO:0000250|UniProtKB:P53264}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (1); Motif (3); Transit peptide (1) |
| Keywords | Hydrolase;Membrane;Mitochondrion;Mitochondrion inner membrane;Reference proteome;Transit peptide |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P53264}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P53264}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53264}; Matrix side {ECO:0000250|UniProtKB:P53264}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 20473289; 20625380; 23697806; 25452419; 28410370; 30726745; |
| Motif | MOTIF 178..182; /note=GXSXG lipase motif; /evidence=ECO:0000250|UniProtKB:P53264; MOTIF 398..403; /note=HXXXXD acyl transferase motif; /evidence=ECO:0000250|UniProtKB:P53264; MOTIF 398..403; /note=HXXXXD motif; /evidence=ECO:0000250|UniProtKB:P53264 |
| Gene Encoded By | |
| Mass | 48,720 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:32935; RHEA:32936 |
| Cross Reference Brenda |