| IED ID | IndEnz0002009319 |
| Enzyme Type ID | protease009319 |
| Protein Name |
Phosphatidylserine decarboxylase 2 proenzyme EC 4.1.1.65 Phosphatidylserine decarboxylase 1, parasitophorous vacuolar Cleaved into: Phosphatidylserine decarboxylase 2 beta chain; Phosphatidylserine decarboxylase 2 alpha chain |
| Gene Name | PSD1pv PSD1 TGGT1_269920 |
| Organism | Toxoplasma gondii (strain ATCC 50853 / GT1) |
| Taxonomic Lineage | cellular organisms Eukaryota Sar Alveolata Apicomplexa Conoidasida Coccidia Eucoccidiorida Eimeriorina Sarcocystidae Toxoplasma Toxoplasma gondii Toxoplasma gondii (strain ATCC 50853 / GT1) |
| Enzyme Sequence | MAKVMRLIIFVCVALVAISVPAASSVQSQQERIRPGFRQQLPSSIRPFSAFRRRGQEASDSVVYLNIVYLRLVGTRQCATGELTVVVHGKALNNATLGDVQTSLTRTFASSLKEPSSTLAIRRWSWKDPLFLMLTLNRRAVRTGTGLPRSTPLYQVAKQRLFVFVRKPTPTSSCRRAALDPRPLYGVPKVGVQDKYTLHVSMDVLGMSLREPLEHQEEEPGPASVSTYAAAQAILDGASSFGIGAFGSAKPNLKQISMYASGAELEKQVYTPTTSQLALFLPSKTFFGVEVTSVSDGTFRIPVSASRLVPFSAMSYMCTGSQTHKLTQTGMNVLEKRVHGKENPPSEGAEVLLNLLAARKPVNGVFEQDPTVVLLQLWRTPEGSESWQETPLMWEFPDTLEAIEDAGEYRSGILSSIAANTRIIGKMAGWLASRSFSRRFIRTLIRLNNIDLEEAFSMSDKDRRHSAADFRSVQEFFTRPINYHVYRDMDPRASIMAPADSLIQNIYTIRPDFKGEISHPIIPQVKSTSFNLREFLYGARQVPPLQLQSPSNRLFVSILYLAPSDYHRVHSPADWRVTSQTYIPGCTPSVSRRNLEAGDLLHRYERTALIGHWDPEKNGQQLFFSVTMVAAMFVGGLRLSWEEEPLGASMRLGRCTRYTESYEKQVDVELCASQEIGAFRFGSTVVMIFEAPEDFDMTSVGQCSHVAAGQPAGYLGQGRERPLQERCNAFRGNFESPFHFWKHLQKTSSVDDILKQNTLAPRAWRQEPGRVWAEVLRATERGLLYGFALSHYLLKRWATENGNLGELVLGQPEVLRQNINGSDSVIREGFRCFAAKDKKQIRLQMSGRQSQVSLTATVTPDEQFLFQHPFYGCVGDEKLGKLVRGIDATWILLPERAVLLTLKVSTGSKQEDGRVLRVATTKIEVQTEPCQGGWEESRVGTTSTTCAIRTVEKREESISEGVLTNGDL |
| Enzyme Length | 968 |
| Uniprot Accession Number | F6N7K6 |
| Absorption | |
| Active Site | ACT_SITE 500; /note=Charge relay system; for autoendoproteolytic cleavage activity; /evidence=ECO:0000250|UniProtKB:B3L2V1; ACT_SITE 570; /note=Charge relay system; for autoendoproteolytic cleavage activity; /evidence=ECO:0000250|UniProtKB:B3L2V1; ACT_SITE 683; /note=Charge relay system; for autoendoproteolytic cleavage activity; /evidence=ECO:0000250|UniProtKB:B3L2V1; ACT_SITE 683; /note=Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity; /evidence=ECO:0000250|UniProtKB:P0A8K1 |
| 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:0000269|PubMed:22563079}; |
| 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. Can act on liposomal and host cell PtdSer. {ECO:0000269|PubMed:22563079}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2. {ECO:0000250|UniProtKB:P39006}. |
| nucleotide Binding | |
| Features | Active site (4); Chain (3); Modified residue (1); Signal peptide (1); Site (1) |
| Keywords | Cytoplasmic vesicle;Decarboxylase;Lipid biosynthesis;Lipid metabolism;Lyase;Phospholipid biosynthesis;Phospholipid metabolism;Pyruvate;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Parasitophorous vacuole {ECO:0000269|PubMed:22563079, ECO:0000269|PubMed:24429285}. Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:22563079}. Note=The protein is stored in dense granules in the parasite and secreted into the parasitophorous vacuole via these granules after host infection. {ECO:0000269|PubMed:22563079}. |
| Modified Residue | MOD_RES 683; /note=Pyruvic acid (Ser); by autocatalysis; /evidence=ECO:0000250|UniProtKB:P0A8K1 |
| 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 (By similarity). 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:0000250|UniProtKB:B3L2V1, ECO:0000250|UniProtKB:P0A8K1, ECO:0000250|UniProtKB:P39006}. |
| Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 108,073 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=67 uM for phosphatidylserine {ECO:0000269|PubMed:22563079}; |
| Metal Binding | |
| Rhea ID | RHEA:20828 |
| Cross Reference Brenda |