| IED ID | IndEnz0002011843 |
| Enzyme Type ID | protease011843 |
| 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 YGR170W |
| 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 | MRIIKGRKRGKNKKPTLILKIHVIQAENIEALKTFNCNPVCFVTTNTFYSQKTNKLKNSNTHWNQTLRIKLPRNPTSEWLRIIVYDALPTGAPPTTPSRPRTTTANTSSSTLSNSGLSSHSHSSRNLNVTSKGNQTSTSINSVSSSATPAPSHSSSSLSTTGPGSTHKNRINSYLYLGEAKISLLDLFKRKDTTTSYKFSIEAQRYHLYDMKGGKDQDSLNCNFLVGDILLGFKLECNVKRTPTFQAFNAWRNELNTYLGRIDRNKARMRSSSSLPPPLEDMLSNSSAVSGNEIRREKPYSDTDLAHDEEVNAEDEIDAEESIEDMNSSGSICTERRYDIDNDTIFDSISEVVSLNDEELDILNDFEEADHPNVPDINVHDIDEDTRISLSSMITALDEYDIVEPEDVAKLPAVSENDITSVDDEESENQQESDEEFDIYNEDEREDSDFQSKEYIGSRLLHLQRGKHNKSYANYLYRRAKSNFFISKKEHAMGVVFMHIGAIKNLPALRNRLSKTNYEMDPFIVISFGRRVFKTSWRKHTLNPEFNEYAAFEVFPHETNFAFSIKVVDKDSFSFNDDVAKCELAWFDMLQQQQHENEWIPYEIPLDLTVEPAHAPKQPVLYSSFKYVSYPFLKKSFWKEAVDTSVNLERLDIIQVMLYLERLGSFTMADSFELFQHFNKSAWAGQSITRSQLVEGLQSWRKSTNFKRIWTCPRCMRSCKPTRNARRSKLVLENDLITHFAICTFSKEHKTLKPSYVSSAFASKRWFSKVLIKLTYGKYALGSNNANILVQDRDTGIIIEEKISAHVKLGMRIIYNGKSPESKKFRSLLKTLSIRQGKKFDSTASAKQIEPFIKFHSLDLSQCRDKDFKTFNEFFYRKLKPGSRLPESNNKEILFSPADSRCTVFPTIQESKEIWVKGRKFSIKKLANNYNPETFNDNNCSIGIFRLAPQDYHRFHSPCNGTIGKPVYVDGEYYTVNPMAVRSELDVFGENIRVIIPIDSPQFGKLLYIPIGAMMVGSILLTCKENDVVESGQELGYFKFGGSTIIIIIPHNNFMFDSDLVKNSSERIETLVKVGMSIGHTSNVNELKRIRIKVDDPKKIERIKRTISVSDENAKSTGNVTWEYHTLREMMNKDFAGL |
| Enzyme Length | 1138 |
| Uniprot Accession Number | P53037 |
| Absorption | |
| Active Site | ACT_SITE 899; /note="Charge relay system; for autoendoproteolytic cleavage activity"; /evidence="ECO:0000250|UniProtKB:B3L2V1, ECO:0000255|HAMAP-Rule:MF_03209"; ACT_SITE 956; /note="Charge relay system; for autoendoproteolytic cleavage activity"; /evidence="ECO:0000250|UniProtKB:B3L2V1, ECO:0000255|HAMAP-Rule:MF_03209"; ACT_SITE 1043; /note="Charge relay system; for autoendoproteolytic cleavage activity"; /evidence="ECO:0000250|UniProtKB:B3L2V1, ECO:0000255|HAMAP-Rule:MF_03209"; ACT_SITE 1043; /note="Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity"; /evidence="ECO:0000250|UniProtKB:P0A8K1, 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, ECO:0000269|PubMed:7890739}; |
| 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:7890740, PubMed:7890739, PubMed:24366873). Phosphatidylethanolamine produced by PSD2 is insufficient to completely provide the PtdEtn pool required by mitochondria under respiratory conditions (PubMed:11294902). PSD2 is also involved in the PtdSer transport step to the site of PtdEtn synthesis on the Golgi/endosome membranes (PubMed:24366873). Required for normal heavy metal resistance (PubMed:20016005). {ECO:0000255|HAMAP-Rule:MF_03209, ECO:0000269|PubMed:11294902, ECO:0000269|PubMed:20016005, ECO:0000269|PubMed:24366873, ECO:0000269|PubMed:7890739, ECO:0000269|PubMed:7890740}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2. {ECO:0000255|HAMAP-Rule:MF_03209, ECO:0000305|PubMed:7890739}. |
| nucleotide Binding | |
| Features | Active site (4); Chain (3); Compositional bias (3); Domain (2); Metal binding (3); Modified residue (1); Mutagenesis (1); Region (3); Sequence conflict (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 | P53844 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_03209, ECO:0000269|PubMed:7890739}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03209, ECO:0000305|PubMed:11104779, ECO:0000305|PubMed:20016005}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03209, ECO:0000305|PubMed:24366873}. Endosome membrane {ECO:0000255|HAMAP-Rule:MF_03209, ECO:0000269|PubMed:20016005}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03209, ECO:0000305|PubMed:11104779, ECO:0000305|PubMed:20016005}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03209, ECO:0000305|PubMed:24366873}. |
| Modified Residue | MOD_RES 1043; /note="Pyruvic acid (Ser); by autocatalysis"; /evidence="ECO:0000250|UniProtKB:P0A8K1, 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 | 10856716; 11180458; 11461929; 11602607; 11786293; 11805826; 12393893; 12441642; 12562848; 12586375; 12857846; 14660568; 15052335; 15522831; 15522832; 15951180; 16036913; 16246067; 16310509; 16429126; 16554755; 16709173; 16807089; 16904369; 17010666; 17976194; 18295604; 18644857; 18836080; 19536198; 19830909; 19841731; 20044027; 21875690; 21926328; 22345606; 22797914; 23027642; 23625917; 23743710; 24007978; 24040173; 24418527; 24520995; 25355612; 25571976; 25810252; 26443863; 27502688; 27521373; 27678054; 27738552; 27746175; 32303746; 6427211; 8852893; 9294443; 9370338; 9885152; |
| Motif | |
| Gene Encoded By | |
| Mass | 130,065 |
| Kinetics | |
| Metal Binding | METAL 571; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00041; METAL 574; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00041; METAL 577; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00041 |
| Rhea ID | RHEA:20828 |
| Cross Reference Brenda |