| IED ID | IndEnz0002008681 |
| Enzyme Type ID | protease008681 |
| Protein Name |
Phosphatidylserine decarboxylase proenzyme EC 4.1.1.65 Cleaved into: Phosphatidylserine decarboxylase beta chain; Phosphatidylserine decarboxylase alpha chain |
| Gene Name | PKH_072580 |
| Organism | Plasmodium knowlesi (strain H) |
| Taxonomic Lineage | cellular organisms Eukaryota Sar Alveolata Apicomplexa Aconoidasida Haemosporida (haemosporidians) Plasmodiidae Plasmodium Plasmodium (Plasmodium) Plasmodium knowlesi Plasmodium knowlesi (strain H) |
| Enzyme Sequence | MKKNGRDNNFYHLYKNKYLITGVTILSFILMFQYKYHEVLTLHDNSENAVQSSKLFWARLLFGRTRSRITGQILKMEIPNTYRLFIFNFLIKYMHINKEEIKYPIESYKSIGDFFSRYIREETRPIGDVSDYSIVSPCDSELIDYGELTSEYLENIKGVKFNVNTFLGSKFQKKHNDGSTKFFYAIFYLSPKKYHHFHAPFNFKYKIRRHISGELFPVFQGMFKFINNLFNINERVILSGEWKGGNVYYAAISAYNVGNIKIINDEELVTNNLRHQLSYMGGDINTKIFDSYKSVEVGDEIGEFRMGSSIVVIFENKKDFSWNVNQNQTVSVGQRLGGIGEPVKEENRFIKIRS |
| Enzyme Length | 354 |
| Uniprot Accession Number | B3L2V1 |
| Absorption | |
| Active Site | ACT_SITE 139; /note="Charge relay system; for autoendoproteolytic cleavage activity"; /evidence="ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000305|PubMed:25724650"; ACT_SITE 198; /note="Charge relay system; for autoendoproteolytic cleavage activity"; /evidence="ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000305|PubMed:25724650"; ACT_SITE 308; /note="Charge relay system; for autoendoproteolytic cleavage activity"; /evidence="ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000305|PubMed:25724650"; ACT_SITE 308; /note="Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity"; /evidence="ECO:0000250|UniProtKB:P0A8K1, ECO:0000255|HAMAP-Rule:MF_03208" |
| Activity Regulation | ACTIVITY REGULATION: Protease activity is inhibited by PMSF. {ECO:0000269|PubMed:25724650}. |
| 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:22057268, ECO:0000269|PubMed:25724650}; |
| 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. {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:22057268}. |
| 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:22057268}. |
| nucleotide Binding | |
| Features | Active site (4); Chain (3); Modified residue (1); Mutagenesis (6); Site (1); Transmembrane (1) |
| Keywords | Decarboxylase;Endoplasmic reticulum;Lipid biosynthesis;Lipid metabolism;Lyase;Membrane;Phospholipid biosynthesis;Phospholipid metabolism;Pyruvate;Reference proteome;Transmembrane;Transmembrane helix;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:22057268}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9GPP8, ECO:0000255|HAMAP-Rule:MF_03208}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03208}. Note=Equally found in the membrane-bound as well as in the soluble fraction. {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:22057268}. |
| Modified Residue | MOD_RES 308; /note="Pyruvic acid (Ser); by autocatalysis"; /evidence="ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:25724650" |
| Post Translational Modification | 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. 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. {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000305|PubMed:25724650}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 41,524 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:20828 |
| Cross Reference Brenda | 4.1.1.65; |