| IED ID | IndEnz0002008110 |
| Enzyme Type ID | protease008110 |
| Protein Name |
Phosphatidylserine decarboxylase proenzyme 2 EC 4.1.1.65 Cleaved into: Phosphatidylserine decarboxylase 2 beta chain; Phosphatidylserine decarboxylase 2 alpha chain |
| Gene Name | PSD2 At5g57190 MUL3.14 |
| Organism | Arabidopsis thaliana (Mouse-ear cress) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress) |
| Enzyme Sequence | MGNGNSREAKESRRSRLRHKLQKFRIHRRHLRSSRNSAGMVIQRTVSAEDFSGIALLTLIGAEMKFKDKWLACVSFGEQTFRTEISDTTQKPIWNSEKKLLLEKNGPSLARVSVFETNRVARNKIIGYCELDIFDFVVQEPESTCKSFNLLDPTSSNVVGSIFLSCAIEDPVETERRFAKRILSIVDYNEDGQLSFSEFSDLIKAFGNLVAANKKEELFKAADLNGDGVVTIDELAALLALQQEQEPIINNCPVCGEALQVSDKLNAMIHMTLCFDEGTGNQVMTGGFLTDRQASYGWMFKLSEWTHLSTYDVGLNTGSSASYIVVIDRKSKRLVEELIDSKIVLSMRAIYQSKIGLRLMDQGAKEILQRLSEKQGKKMSSVESAQKIPRFLEFFKDQINMAEVKYPLQHFKTFNEFFIRELKPGARPIACMNRNDVAVCAADCRLMAFQSVEDSTRFWIKGKKFSIRGLLGKNVNPNAFLDGSLVIFRLAPQDYHRFHVPVSGVIEQFVDVSGSLYTVNPIAVNSKYCNVFTENKRTVAIISTAEFGKVAFVAIGATMVGSINFVRKEGEHVKKGDELGYFSFGGSTVICVFEKDAIGIDNDLLVNSGRSLETLVSVGMQLGVSTRTFARSTLI |
| Enzyme Length | 635 |
| Uniprot Accession Number | F4KAK5 |
| Absorption | |
| Active Site | ACT_SITE 443; /note=Charge relay system; for autoendoproteolytic cleavage activity; /evidence=ECO:0000255|HAMAP-Rule:MF_03209; ACT_SITE 499; /note=Charge relay system; for autoendoproteolytic cleavage activity; /evidence=ECO:0000255|HAMAP-Rule:MF_03209; ACT_SITE 587; /note=Charge relay system; for autoendoproteolytic cleavage activity; /evidence=ECO:0000255|HAMAP-Rule:MF_03209; ACT_SITE 587; /note=Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity; /evidence=ECO:0000255|HAMAP-Rule:MF_03209 |
| 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_03209}; |
| 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. Contributes only to a minor proportion of PtdEtn production. {ECO:0000255|HAMAP-Rule:MF_03209, ECO:0000269|PubMed:17449644}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2. {ECO:0000255|HAMAP-Rule:MF_03209}. |
| nucleotide Binding | |
| Features | Active site (4); Chain (3); Domain (3); Erroneous gene model prediction (1); Erroneous initiation (1); Metal binding (9); Modified residue (1); Sequence conflict (1); Site (1) |
| Keywords | Calcium;Decarboxylase;Lipid biosynthesis;Lipid metabolism;Lyase;Membrane;Metal-binding;Phospholipid biosynthesis;Phospholipid metabolism;Pyruvate;Reference proteome;Repeat;Vacuole;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000305|PubMed:17449644}; Peripheral membrane protein {ECO:0000305|PubMed:17449644}. Note=Tonoplast. |
| Modified Residue | MOD_RES 587; /note=Pyruvic acid (Ser); by autocatalysis; /evidence=ECO:0000255|HAMAP-Rule:MF_03209 |
| 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_03209}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11461929; 12372144; 12912986; 14722088; 23505340; 9301097; |
| Motif | |
| Gene Encoded By | |
| Mass | 71,000 |
| Kinetics | |
| Metal Binding | METAL 187; /note=Calcium 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03209; METAL 189; /note=Calcium 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03209; METAL 191; /note=Calcium 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03209; METAL 193; /note=Calcium 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03209; METAL 198; /note=Calcium 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03209; METAL 223; /note=Calcium 2; /evidence=ECO:0000255|HAMAP-Rule:MF_03209; METAL 225; /note=Calcium 2; /evidence=ECO:0000255|HAMAP-Rule:MF_03209; METAL 227; /note=Calcium 2; /evidence=ECO:0000255|HAMAP-Rule:MF_03209; METAL 234; /note=Calcium 2; /evidence=ECO:0000255|HAMAP-Rule:MF_03209 |
| Rhea ID | RHEA:20828 |
| Cross Reference Brenda | 4.1.1.65; |