| IED ID | IndEnz0002008777 |
| Enzyme Type ID | protease008777 |
| 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 CAALFM_C504680WA CaO19.3954 orf19.3954 |
| Organism | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Debaryomycetaceae Candida/Lodderomyces clade Candida Candida albicans (Yeast) Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
| Enzyme Sequence | MRSSGYLNSNNGSSSSLESTNVNKSTDKNQLYLKVVCNCATDLVPQDTTGTGSESKKAYSSSKSINPVLVVQLNNTIKSTSKKLNTNQPSWNDELYMPLKNQDDSSLLIFSVWDKHTRYKNYLGELRLNVKDIFVDNGNFVDKTELKWYHLNSNTKYHSFVTGSILAGFELVIKNKKKRFHSSYNDKFQQLSIDSDVESAFKKWLSSLTKPTIYSVNNKINPNDQGFYDDELVNEFELESVLTERSKKSHLNVPGGNGLLSVPGDDCHDAGSFSDASFLSDGGYASDASANLFDQKETSSDSKKSRIKSKMRLRRSKQEYENFELASRQVLGVVFIEIVSCEDLPPYKNFTRTSFDMDPFVVVSFGKKTFRTGWKRHTLNPVFNERLAFELLPHESNFSIQFLVLDKDHFSFHDNVAHISLPLRTLTEYATAKPTEGDSSDVNTSDSTSFSQTGNGFTTEDTEFPENDSVQIIENETPSNKQSRKRYLSRKKVVGTQLDLKKFKAMSLSLQLHDQKYIGKYAPKLKIRVRFETYTELRKKFWRVLLEESNSTPENRDSCDYIELISLLDTLGCVNSDELVELFYSNLGKSSWGGDLLTFDEIIDQMETYVNQNVESGKVKIFEFEKCPICNEKRVSKKQDLDIITHFAICASKDWSVVGKLLSSSYVTPTQATKKWFTKALIKLTYGKYKLGGNSANILVQDRMTGIIVEEKMSVYVRLGIRLLYKGLDKARSKRVRILLKNMSIKQGKKFDAPQSKSDIASFIKFHKLDLDECEIDDPSQFATFNDFFYRKLKPGAREIEDEKNSKIVTSPADCRSVVFESIDKATQLWIKGAGFTIPKLIHNDHSMRVSSYTLGIFRLAPQDYHRFHSPVDGVIESIKHIDGEYYTVNPMAIRSELDVFGENVRTIVTIKTKDFGNIYFIAVGAMMVGSIVLTKDTGYEISKGEELGYFKFGGSTVLLLIESDKFKFDTDLVKNSSSGLETLLRVGQSIGHSPDVEEYKRDHISFDKLDKSKQLRLIRVLTGGDLKDKHKLSNWEATKIDMEDFQEIEDEEVFDKDMPDEDASIKSED |
| Enzyme Length | 1070 |
| Uniprot Accession Number | Q5AK66 |
| Absorption | |
| Active Site | ACT_SITE 814; /note=Charge relay system; for autoendoproteolytic cleavage activity; /evidence=ECO:0000255|HAMAP-Rule:MF_03209; ACT_SITE 869; /note=Charge relay system; for autoendoproteolytic cleavage activity; /evidence=ECO:0000255|HAMAP-Rule:MF_03209; ACT_SITE 956; /note=Charge relay system; for autoendoproteolytic cleavage activity; /evidence=ECO:0000255|HAMAP-Rule:MF_03209; ACT_SITE 956; /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 (By similarity). Important for virulence (PubMed:20132453). {ECO:0000250|UniProtKB:P53037, ECO:0000255|HAMAP-Rule:MF_03209, ECO:0000269|PubMed:20132453}. |
| 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 (2); Metal binding (3); Modified residue (1); Region (2); Site (1) |
| Keywords | Calcium;Decarboxylase;Endosome;Golgi apparatus;Lipid biosynthesis;Lipid metabolism;Lyase;Membrane;Metal-binding;Phospholipid biosynthesis;Phospholipid metabolism;Pyruvate;Reference proteome;Repeat;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_03209}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03209}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03209}. Endosome membrane {ECO:0000255|HAMAP-Rule:MF_03209}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03209}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03209}. |
| Modified Residue | MOD_RES 956; /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 | - |
| Motif | |
| Gene Encoded By | |
| Mass | 121,666 |
| Kinetics | |
| Metal Binding | METAL 408; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00041; METAL 411; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00041; METAL 414; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00041 |
| Rhea ID | RHEA:20828 |
| Cross Reference Brenda | 4.1.1.65; |