| IED ID | IndEnz0005000391 |
| Enzyme Type ID | lipase000391 |
| Protein Name |
NADPH-dependent 1-acyldihydroxyacetone phosphate reductase ADR EC 1.1.1.101 1-acyl DHAP reductase Acyl/alkyl DHAP reductase Acylglycerone-phosphate reductase Triacylglycerol lipase ayr1 TAG lipase EC 3.1.1.3 |
| Gene Name | ayr1 SPAC23D3.11 |
| 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 | MEAEKFVLITGCSEGGIGNALALKFHQEGFQVLATARQVERMDNLTKAGLQTLKLDVTDEDSVREVEQEVRKFTNGSLHYLINNAGAPCSAPAIDLDIEDVSKVMDVNFYGVIRMNKAFQHQLIRAKGTIVNVNSLVSYVPFAFNAAYNASKAALLAYSNTLRIELAPFGVQVTSIMTGGVQTKIQSKPLGTMTEAAIPENSIYYPYRKLILENRNPVEKFVTIEEFADAAYPQLVGRGRWYQLFKPGVRPAQIWAGYMSSAGRVGSMLPVEVFSMSVRLIVKLPSTAVWRDHTVD |
| Enzyme Length | 296 |
| Uniprot Accession Number | Q09851 |
| Absorption | |
| Active Site | ACT_SITE 13; /note=Nucleophile; for lipase activity; /evidence=ECO:0000250|UniProtKB:P40471; ACT_SITE 148; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10001 |
| Activity Regulation | |
| Binding Site | BINDING 135; /note=Substrate; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphate + NADP(+) = 1-hexadecanoylglycerone 3-phosphate + H(+) + NADPH; Xref=Rhea:RHEA:17341, ChEBI:CHEBI:15378, ChEBI:CHEBI:57518, ChEBI:CHEBI:57783, ChEBI:CHEBI:58303, ChEBI:CHEBI:58349; EC=1.1.1.101; Evidence={ECO:0000250|UniProtKB:P40471}; CATALYTIC ACTIVITY: Reaction=a 1-acylglycerone 3-phosphate + H(+) + NADPH = a 1-acyl-sn-glycero-3-phosphate + NADP(+); Xref=Rhea:RHEA:33375, ChEBI:CHEBI:15378, ChEBI:CHEBI:57534, ChEBI:CHEBI:57783, ChEBI:CHEBI:57970, ChEBI:CHEBI:58349; Evidence={ECO:0000250|UniProtKB:P40471};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33376; Evidence={ECO:0000250|UniProtKB:P40471}; CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000250|UniProtKB:P40471};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045; Evidence={ECO:0000250|UniProtKB:P40471}; |
| DNA Binding | |
| EC Number | 1.1.1.101; 3.1.1.3 |
| Enzyme Function | FUNCTION: Can convert acyl and alkyl dihydroxyacetone-phosphate (DHAP) into glycerolipids and ether lipids, respectively. Required for the biosynthesis of phosphatidic acid via the DHAP pathway, where it reduces 1-acyl DHAP to lysophosphatidic acid (LPA). Also has triacylglycerol (TAG) lipase activity. Involved in the mobilization of the non-polar storage lipids triacylglycerols (TAGs) from lipid particles by hydrolysis of TAGs. Lipolysis of TAG by AYR1 is essential for starvation-induced autophagy. Forms an NADPH-regulated cation-selective channel in the mitochondrial outer membrane. {ECO:0000250|UniProtKB:P40471}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 8..33; /note=NAD or NADP; /evidence=ECO:0000250; NP_BIND 9..17; /note=NAD; /evidence=ECO:0000250|UniProtKB:Q92506; NP_BIND 55..57; /note=NAD; /evidence=ECO:0000250|UniProtKB:Q92506; NP_BIND 148..152; /note=NAD; /evidence=ECO:0000250|UniProtKB:Q92506; NP_BIND 181..183; /note=NAD; /evidence=ECO:0000250|UniProtKB:Q92506 |
| Features | Active site (2); Binding site (1); Chain (1); Motif (1); Nucleotide binding (5) |
| Keywords | Cytoplasm;Endoplasmic reticulum;Golgi apparatus;Hydrolase;Lipid degradation;Lipid droplet;Lipid metabolism;Membrane;Mitochondrion;Mitochondrion outer membrane;NAD;NADP;Oxidoreductase;Reference proteome;Vacuole |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Lipid droplet {ECO:0000250|UniProtKB:P40471}. Cytoplasm {ECO:0000269|PubMed:16823372}. Vacuole {ECO:0000269|PubMed:16823372}. Endoplasmic reticulum {ECO:0000269|PubMed:16823372}. Golgi apparatus {ECO:0000269|PubMed:16823372}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:P40471}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 20473289; 23697806; 26412298; 27887640; |
| Motif | MOTIF 11..15; /note=GXSXG; /evidence=ECO:0000250|UniProtKB:P40471 |
| Gene Encoded By | |
| Mass | 32,731 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:17341; RHEA:33375; RHEA:33376; RHEA:12044; RHEA:12045 |
| Cross Reference Brenda |