| IED ID | IndEnz0002007385 |
| Enzyme Type ID | protease007385 |
| Protein Name |
Phosphatidylserine decarboxylase proenzyme 1, mitochondrial EC 4.1.1.65 Cleaved into: Phosphatidylserine decarboxylase 1 beta chain; Phosphatidylserine decarboxylase 1 alpha chain |
| Gene Name | PSD1 YNL169C N1692 |
| 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 | MSIMPVKNALAQGRTLLMGRMPAVKFSTRMQLRNRTAVLWNRKFSTRLFVQQRRSSGEIVDRAKAAAANSGRKQVSMKWVVLTSFTIVLGTILLVSRNDSTEEDATEGKKGRRTRKIKIFNNNWLFFCYSTLPLNAMSRLWGQVNSLTLPIWVRPWGYRLYSFLFGVNLDEMEDPDLTHYANLSEFFYRNIKPGTRPVAQGEDVIASPSDGKILQVGIINSETGEIEQVKGMTYSIKEFLGTHSHPLMSKSASSLDLTSDEEKHREFARVNRIQLAGSEDTEQPLLNFKNEGDQSVREFKPSVSKNIHLLSQLSLNYFSNGFSCSEPHDTELFFAVIYLAPGDYHHFHSPVDWVCKVRRHFPGDLFSVAPYFQRNFPNLFVLNERVALLGSWKYGFFSMTPVGATNVGSIKLNFDQEFVTNSKSDKHLEPHTCYQAVYENASKILGGMPLVKGEEMGGFELGSTVVLCFEAPTEFKFDVRVGDKVKMGQKLGIIGKNDLK |
| Enzyme Length | 500 |
| Uniprot Accession Number | P39006 |
| Absorption | |
| Active Site | ACT_SITE 210; /note=Charge relay system; for autoendoproteolytic cleavage activity; /evidence=ECO:0000255|HAMAP-Rule:MF_03208; ACT_SITE 348; /note=Charge relay system; for autoendoproteolytic cleavage activity; /evidence=ECO:0000255|HAMAP-Rule:MF_03208; ACT_SITE 463; /note=Charge relay system; for autoendoproteolytic cleavage activity; /evidence=ECO:0000255|HAMAP-Rule:MF_03208; ACT_SITE 463; /note=Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity; /evidence=ECO:0000255|HAMAP-Rule:MF_03208 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2; Xref=Rhea:RHEA:20828, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57262, ChEBI:CHEBI:64612; EC=4.1.1.65; Evidence={ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:23124206, ECO:0000269|PubMed:6427211, ECO:0000305|PubMed:17976194}; |
| DNA Binding | |
| EC Number | 4.1.1.65 |
| Enzyme Function | FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine (PubMed:8227017, PubMed:8407984, PubMed:17976194, PubMed:23124206, PubMed:25829489). Phosphatidylethanolamine formed in the mitochondria is exported to other membranes to fullfill their requirements for PtdEtn (PubMed:8530379, PubMed:11294902). Required for normal mitochondrial morphology and proper mitochondrial fusion during yeast mating (PubMed:23045528). {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:11294902, ECO:0000269|PubMed:17976194, ECO:0000269|PubMed:23045528, ECO:0000269|PubMed:23124206, ECO:0000269|PubMed:25829489, ECO:0000269|PubMed:8227017, ECO:0000269|PubMed:8407984, ECO:0000269|PubMed:8530379}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2. {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000305|PubMed:8407984}. |
| nucleotide Binding | |
| Features | Active site (4); Chain (3); Modified residue (1); Mutagenesis (7); Site (1); Topological domain (2); Transit peptide (1); Transmembrane (1) |
| Keywords | Decarboxylase;Lipid biosynthesis;Lipid metabolism;Lyase;Membrane;Mitochondrion;Mitochondrion inner membrane;Phospholipid biosynthesis;Phospholipid metabolism;Pyruvate;Reference proteome;Transit peptide;Transmembrane;Transmembrane helix;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase 1 beta chain]: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:22984266, ECO:0000269|PubMed:23124206, ECO:0000269|PubMed:3005242}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000305|PubMed:22984266}; Intermembrane side {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:22984266, ECO:0000269|PubMed:23124206}.; SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase 1 alpha chain]: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:22984266, ECO:0000269|PubMed:23124206, ECO:0000269|PubMed:3005242}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:22984266}; Intermembrane side {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:22984266, ECO:0000269|PubMed:23124206}. Note=Anchored to the mitochondrial inner membrane through its interaction with the integral membrane beta chain. {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:22984266}. |
| Modified Residue | MOD_RES 463; /note=Pyruvic acid (Ser); by autocatalysis; /evidence=ECO:0000255|HAMAP-Rule:MF_03208 |
| Post Translational Modification | PTM: The precursor is imported via the TOM complex into mitochondria, where the N-terminal presequence is cleaved by the matrix-located proteases MPP (MAS1-MAS2) and OCT1. {ECO:0000269|PubMed:22984266, ECO:0000305|PubMed:17976194}.; PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme (PubMed:25829489, PubMed:30858161). The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase (By similarity). {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000305|PubMed:18644857, ECO:0000305|PubMed:30858161}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10856716; 11180458; 11283351; 11461929; 11470244; 11602607; 11786293; 11805837; 12441642; 12562848; 12586375; 12589040; 12857846; 14690591; 15052335; 15273086; 15522831; 15522832; 15951180; 16036913; 16093310; 16246067; 16310509; 16429126; 16709173; 16807089; 16904369; 17010666; 18295604; 18836080; 1917869; 19221197; 19363031; 19830909; 19930686; 20044027; 20410371; 21306442; 21926328; 21964439; 21967054; 22345606; 22433850; 22797914; 23027642; 23042933; 23625917; 23631861; 23743710; 23956814; 24007978; 24146988; 24190879; 24201294; 24418527; 24520995; 24771456; 24866973; 25201965; 25355612; 25487302; 25571976; 25761633; 25810252; 25833713; 26385920; 26443863; 26480301; 2692476; 27226479; 27502688; 27521373; 27678054; 27693354; 27736935; 27738552; 27746175; 29126902; 30459179; 7890739; 7890740; 8852893; 9294443; 9370338; 9885152; |
| Motif | |
| Gene Encoded By | |
| Mass | 56,595 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:20828 |
| Cross Reference Brenda | 4.1.1.65; |