ID PSD1_YEAST Reviewed; 500 AA. AC P39006; D6W113; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 10-JUN-2026, entry version 197. DE RecName: Full=Phosphatidylserine decarboxylase proenzyme 1, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000305|PubMed:8227017}; DE EC=4.1.1.65 {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:6427211, ECO:0000305|PubMed:17976194}; DE Contains: DE RecName: Full=Phosphatidylserine decarboxylase 1 beta chain {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000305|PubMed:18644857}; DE Contains: DE RecName: Full=Phosphatidylserine decarboxylase 1 alpha chain {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000305|PubMed:18644857}; DE Flags: Precursor; GN Name=PSD1 {ECO:0000255|HAMAP-Rule:MF_03208, GN ECO:0000303|PubMed:8227017}; GN OrderedLocusNames=YNL169C {ECO:0000312|SGD:S000005113}; GN ORFNames=N1692; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION. RC STRAIN=ATCC 204510 / AB320; RX PubMed=8227017; DOI=10.1016/s0021-9258(19)74506-2; RA Clancey C.J., Chang S.-C., Dowhan W.; RT "Cloning of a gene (PSD1) encoding phosphatidylserine decarboxylase from RT Saccharomyces cerevisiae by complementation of an Escherichia coli RT mutant."; RL J. Biol. Chem. 268:24580-24590(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY. RX PubMed=8407984; DOI=10.1016/s0021-9258(19)36940-6; RA Trotter P.J., Pedretti J., Voelker D.R.; RT "Phosphatidylserine decarboxylase from Saccharomyces cerevisiae. Isolation RT of mutants, cloning of the gene, and creation of a null allele."; RL J. Biol. Chem. 268:21416-21424(1993). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169873; DOI=10.1038/387s093; RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F., RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its RT evolutionary implications."; RL Nature 387:93-98(1997). RN [4] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-174. RC STRAIN=ATCC 96604 / S288c / FY1679; RX PubMed=8686380; RX DOI=10.1002/(sici)1097-0061(199602)12:2<169::aid-yea894>3.0.co;2-b; RA Nasr F., Becam A.-M., Herbert C.J.; RT "The sequence of 36.8 kb from the left arm of chromosome XIV reveals 24 RT complete open reading frames: 18 correspond to new genes, one of which RT encodes a protein similar to the human myotonic dystrophy kinase."; RL Yeast 12:169-175(1996). RN [6] RP CATALYTIC ACTIVITY. RX PubMed=6427211; DOI=10.1016/s0021-9258(20)82136-x; RA Carson M.A., Emala M., Hogsten P., Waechter C.J.; RT "Coordinate regulation of phosphatidylserine decarboxylase activity and RT phospholipid N-methylation in yeast."; RL J. Biol. Chem. 259:6267-6273(1984). RN [7] RP SUBCELLULAR LOCATION. RX PubMed=3005242; DOI=10.1128/jb.165.3.901-910.1986; RA Kuchler K., Daum G., Paltauf F.; RT "Subcellular and submitochondrial localization of phospholipid-synthesizing RT enzymes in Saccharomyces cerevisiae."; RL J. Bacteriol. 165:901-910(1986). RN [8] RP FUNCTION. RX PubMed=8530379; DOI=10.1074/jbc.270.50.29836; RA Achleitner G., Zweytick D., Trotter P.J., Voelker D.R., Daum G.; RT "Synthesis and intracellular transport of aminoglycerophospholipids in RT permeabilized cells of the yeast, Saccharomyces cerevisiae."; RL J. Biol. Chem. 270:29836-29842(1995). RN [9] RP INDUCTION, AND DISRUPTION PHENOTYPE. RX PubMed=9294443; DOI=10.1128/jb.179.18.5843-5848.1997; RA Griac P.; RT "Regulation of yeast phospholipid biosynthetic genes in phosphatidylserine RT decarboxylase mutants."; RL J. Bacteriol. 179:5843-5848(1997). RN [10] RP FUNCTION. RX PubMed=11294902; DOI=10.1091/mbc.12.4.997; RA Birner R., Buergermeister M., Schneiter R., Daum G.; RT "Roles of phosphatidylethanolamine and of its several biosynthetic pathways RT in Saccharomyces cerevisiae."; RL Mol. Biol. Cell 12:997-1007(2001). RN [11] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [12] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [13] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC STRAIN=ATCC 76625 / YPH499; RX PubMed=14576278; DOI=10.1073/pnas.2135385100; RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., RA Pfanner N., Meisinger C.; RT "The proteome of Saccharomyces cerevisiae mitochondria."; RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003). RN [14] RP FUNCTION, CATALYTIC ACTIVITY, AND PROTEOLYTIC PROCESSING. RX PubMed=17976194; DOI=10.1111/j.1742-4658.2007.06138.x; RA Nebauer R., Schuiki I., Kulterer B., Trajanoski Z., Daum G.; RT "The phosphatidylethanolamine level of yeast mitochondria is affected by RT the mitochondrial components Oxa1p and Yme1p."; RL FEBS J. 274:6180-6190(2007). RN [15] RP PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF 461-LEU--SER-463. RX PubMed=18644857; DOI=10.1128/mcb.00405-08; RA Gulshan K., Schmidt J.A., Shahi P., Moye-Rowley W.S.; RT "Evidence for the bifunctional nature of mitochondrial phosphatidylserine RT decarboxylase: role in Pdr3-dependent retrograde regulation of PDR5 RT expression."; RL Mol. Cell. Biol. 28:5851-5864(2008). RN [16] RP MUTAGENESIS OF SER-463 AND 81-VAL--SER-100, SUBCELLULAR LOCATION, AND RP TOPOLOGY. RX PubMed=22984266; DOI=10.1074/jbc.m112.398107; RA Horvath S.E., Boettinger L., Voegtle F.N., Wiedemann N., Meisinger C., RA Becker T., Daum G.; RT "Processing and topology of the yeast mitochondrial phosphatidylserine RT decarboxylase 1."; RL J. Biol. Chem. 287:36744-36755(2012). RN [17] RP FUNCTION. RX PubMed=23045528; DOI=10.1074/jbc.m112.399428; RA Chan E.Y., McQuibban G.A.; RT "Phosphatidylserine decarboxylase 1 (Psd1) promotes mitochondrial fusion by RT regulating the biophysical properties of the mitochondrial membrane and RT alternative topogenesis of mitochondrial genome maintenance protein 1 RT (Mgm1)."; RL J. Biol. Chem. 287:40131-40139(2012). RN [18] RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION. RX PubMed=23124206; DOI=10.1074/jbc.m112.390997; RA Tamura Y., Onguka O., Itoh K., Endo T., Iijima M., Claypool S.M., RA Sesaki H.; RT "Phosphatidylethanolamine biosynthesis in mitochondria: phosphatidylserine RT (PS) trafficking is independent of a PS decarboxylase and intermembrane RT space proteins UPS1P and UPS2P."; RL J. Biol. Chem. 287:43961-43971(2012). RN [19] RP DISRUPTION PHENOTYPE. RX PubMed=24146988; DOI=10.1371/journal.pone.0077380; RA Gsell M., Mascher G., Schuiki I., Ploier B., Hrastnik C., Daum G.; RT "Transcriptional response to deletion of the phosphatidylserine RT decarboxylase Psd1p in the yeast Saccharomyces cerevisiae."; RL PLoS ONE 8:e77380-e77380(2013). RN [20] RP FUNCTION, AND MUTAGENESIS OF LEU-461; GLY-462; SER-463 AND THR-464. RX PubMed=25829489; DOI=10.1074/jbc.m115.641118; RA Onguka O., Calzada E., Ogunbona O.B., Claypool S.M.; RT "Phosphatidylserine decarboxylase 1 autocatalysis and function does not RT require a mitochondrial-specific factor."; RL J. Biol. Chem. 290:12744-12752(2015). RN [21] RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF SER-463; 475-PHE--LYS-486; RP 479-VAL--VAL-481; 480-ARG--LYS-486; 480-ARG--VAL-485; 482-GLY--LYS-484; RP GLY-482; 483-ASP-LYS-484; LYS-486; GLY-488; 491-LEU-GLY-492 AND GLY-492. RX PubMed=28473294; DOI=10.1016/j.bbalip.2017.04.007; RA Di Bartolomeo F., Doan K.N., Athenstaedt K., Becker T., Daum G.; RT "Involvement of a putative substrate binding site in the biogenesis and RT assembly of phosphatidylserine decarboxylase 1 from Saccharomyces RT cerevisiae."; RL Biochim. Biophys. Acta 1862:716-725(2017). RN [22] {ECO:0000305} RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, GLYCOSYLATION AT RP ASN-34, AND MUTAGENESIS OF SER-463. RC STRAIN=ATCC 200060 / W303 {ECO:0000303|PubMed:29290583}; RX PubMed=29290583; DOI=10.1016/j.devcel.2017.11.023; RA Friedman J.R., Kannan M., Toulmay A., Jan C.H., Weissman J.S., Prinz W.A., RA Nunnari J.; RT "Lipid Homeostasis Is Maintained by Dual Targeting of the Mitochondrial PE RT Biosynthesis Enzyme to the ER."; RL Dev. Cell 44:261-270(2018). RN [23] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=30510114; DOI=10.1242/jcs.221655; RA Vigie P., Cougouilles E., Bhatia-Kissova I., Salin B., Blancard C., RA Camougrand N.; RT "The mitochondrial phosphatidylserine decarboxylase Psd1 is involved in RT nitrogen starvation-induced mitophagy in yeast."; RL J. Cell Sci. 132:jcs221655-jcs221655(2019). RN [24] RP PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF ARG-358. RX PubMed=30858161; DOI=10.26508/lsa.201900353; RG Care4Rare Canada Consortium; RA Zhao T., Goedhart C.M., Sam P.N., Sabouny R., Lingrell S., Cornish A.J., RA Lamont R.E., Bernier F.P., Sinasac D., Parboosingh J.S., Vance J.E., RA Claypool S.M., Innes A.M., Shutt T.E.; RT "PISD is a mitochondrial disease gene causing skeletal dysplasia, RT cataracts, and white matter changes."; RL Life. Sci Alliance 2:0-0(2019). RN [25] {ECO:0000305} RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=30926815; DOI=10.1038/s41467-019-09425-1; RA Calzada E., Avery E., Sam P.N., Modak A., Wang C., McCaffery J.M., Han X., RA Alder N.N., Claypool S.M.; RT "Phosphatidylethanolamine made in the inner mitochondrial membrane is RT essential for yeast cytochrome bc1 complex function."; RL Nat. Commun. 10:1432-1432(2019). RN [26] {ECO:0000305} RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-189; ARG-196; ASP-210; RP LYS-230; HIS-345; HIS-346; ARG-385; 402-VAL--THR-405; 407-VAL--ILE-410; RP 461-LEU--SER-463 AND SER-463. RC STRAIN=ATCC 200060 / W303 {ECO:0000303|PubMed:33718843}, and GA74-1A RC {ECO:0000303|PubMed:33718843}; RX PubMed=33718843; DOI=10.1016/j.isci.2021.102196; RA Sam P.N., Calzada E., Acoba M.G., Zhao T., Watanabe Y., Nejatfard A., RA Trinidad J.C., Shutt T.E., Neal S.E., Claypool S.M.; RT "Impaired phosphatidylethanolamine metabolism activates a reversible stress RT response that detects and resolves mutant mitochondrial precursors."; RL IScience 24:102196-102196(2021). RN [27] {ECO:0000305} RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE. RC STRAIN=ATCC 200060 / W303 {ECO:0000303|PubMed:34818062}; RX PubMed=34818062; DOI=10.1091/mbc.e21-11-0558-t; RA Gok M.O., Speer N.O., Henne W.M., Friedman J.R.; RT "ER-localized phosphatidylethanolamine synthase plays a conserved role in RT lipid droplet formation."; RL Mol. Biol. Cell 33:ar11-ar11(2022). CC -!- FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) CC from phosphatidylserine (PtdSer). Plays a central role in phospholipid CC metabolism and in the interorganelle trafficking of phosphatidylserine CC (PubMed:17976194, PubMed:23124206, PubMed:25829489, PubMed:29290583, CC PubMed:8227017, PubMed:8407984). Phosphatidylethanolamine formed in the CC mitochondria is exported to other membranes to fullfill their CC requirements for PtdEtn (PubMed:11294902, PubMed:29290583, CC PubMed:8530379). Required for normal mitochondrial morphology and CC proper mitochondrial fusion during yeast mating (PubMed:23045528). CC Involved in lipid droplet biogenesis at the endoplasmic reticulum CC membrane (PubMed:34818062). Required for induction of mitophagy during CC nitrogen starvation (PubMed:30510114). Appears to play a specific role CC in supporting respiratory complex III activity (PubMed:30926815). CC {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:11294902, CC ECO:0000269|PubMed:17976194, ECO:0000269|PubMed:23045528, CC ECO:0000269|PubMed:23124206, ECO:0000269|PubMed:25829489, CC ECO:0000269|PubMed:29290583, ECO:0000269|PubMed:30926815, CC ECO:0000269|PubMed:34818062, ECO:0000269|PubMed:8227017, CC ECO:0000269|PubMed:8407984, ECO:0000269|PubMed:8530379}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2- CC diacyl-sn-glycero-3-phosphoethanolamine + CO2; Xref=Rhea:RHEA:20828, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57262, CC ChEBI:CHEBI:64612; EC=4.1.1.65; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03208, ECO:0000269|PubMed:23124206, CC ECO:0000269|PubMed:6427211, ECO:0000305|PubMed:17976194, CC ECO:0000305|PubMed:8407984}; CC -!- COFACTOR: CC Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03208}; CC Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP- CC Rule:MF_03208}; CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine CC biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step CC 2/2. {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000305|PubMed:8407984}. CC -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit and a CC small pyruvoyl-containing alpha subunit. {ECO:0000255|HAMAP- CC Rule:MF_03208}. CC -!- SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase 1 beta chain]: CC Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208, CC ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:22984266, CC ECO:0000269|PubMed:23124206, ECO:0000269|PubMed:29290583, CC ECO:0000269|PubMed:3005242, ECO:0000269|PubMed:33718843, CC ECO:0000305|PubMed:34818062}; Single-pass membrane protein CC {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000305|PubMed:22984266}; CC Intermembrane side {ECO:0000255|HAMAP-Rule:MF_03208, CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, CC ECO:0000269|PubMed:22984266, ECO:0000269|PubMed:23124206}. CC -!- SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase 1 alpha chain]: CC Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208, CC ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:22984266, CC ECO:0000269|PubMed:23124206, ECO:0000269|PubMed:29290583, CC ECO:0000269|PubMed:3005242, ECO:0000305|PubMed:34818062}; Peripheral CC membrane protein {ECO:0000255|HAMAP-Rule:MF_03208, CC ECO:0000269|PubMed:22984266}; Intermembrane side {ECO:0000255|HAMAP- CC Rule:MF_03208, ECO:0000269|PubMed:14562095, CC ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:22984266, CC ECO:0000269|PubMed:23124206}. Note=Anchored to the mitochondrial inner CC membrane through its interaction with the integral membrane beta chain. CC {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:22984266}. CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:34818062}. CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:29290583, CC ECO:0000269|PubMed:34818062}. Note=Localizes to sites of lipid droplet CC formation on the endoplasmic reticulum membrane. CC {ECO:0000269|PubMed:34818062}. CC -!- INDUCTION: Repressed by inositol. {ECO:0000269|PubMed:9294443}. CC -!- PTM: Glycosylated at Asn-34 in the endoplasmic reticulum. CC {ECO:0000269|PubMed:29290583}. CC -!- PTM: The precursor is imported via the TOM complex into mitochondria, CC where the N-terminal presequence is cleaved by the matrix-located CC proteases MPP (MAS1-MAS2) and OCT1. {ECO:0000269|PubMed:22984266, CC ECO:0000305|PubMed:17976194}. CC -!- PTM: Is synthesized initially as an inactive proenzyme. Formation of CC the active enzyme involves a self-maturation process in which the CC active site pyruvoyl group is generated from an internal serine residue CC via an autocatalytic post-translational modification. Two non-identical CC subunits are generated from the proenzyme in this reaction, and the CC pyruvate is formed at the N-terminus of the alpha chain, which is CC derived from the carboxyl end of the proenzyme (PubMed:25829489, CC PubMed:30858161). The autoendoproteolytic cleavage occurs by a CC canonical serine protease mechanism, in which the side chain hydroxyl CC group of the serine supplies its oxygen atom to form the C-terminus of CC the beta chain, while the remainder of the serine residue undergoes an CC oxidative deamination to produce ammonia and the pyruvoyl prosthetic CC group on the alpha chain. During this reaction, the Ser that is part of CC the protease active site of the proenzyme becomes the pyruvoyl CC prosthetic group, which constitutes an essential element of the active CC site of the mature decarboxylase (By similarity). {ECO:0000255|HAMAP- CC Rule:MF_03208, ECO:0000305|PubMed:18644857, CC ECO:0000305|PubMed:30858161}. CC -!- DISRUPTION PHENOTYPE: The cellular level of phosphatidylethanolamine is CC decreased, and phosphatidylcholine levels are increased CC (PubMed:24146988, PubMed:30926815, PubMed:9294443). Decreases induction CC of mitophagy in nitrogen starvation following growth on a respiratory CC carbon source; recruitment of ATG8 to mitochondria is impaired CC (PubMed:30510114). Growth on non-fermentable carbon sources is severely CC decreased (lactate, ethanol and glycerol) (PubMed:24146988, CC PubMed:30926815, PubMed:34818062). Growth on the fermentable carbon CC source galactose is severely decreased (PubMed:28473294). Increases RNA CC level of genes involved in transport, generation of precursor CC metabolites and energy, carbohydrate metabolism, and stress responses CC (PubMed:24146988). Leads to respiratory defects; respiratory complex CC III and IV activity is impaired (PubMed:30926815). Simultaneous CC disruption of PSD2 exacerbates respiratory defects (PubMed:30926815). CC {ECO:0000269|PubMed:24146988, ECO:0000269|PubMed:28473294, CC ECO:0000269|PubMed:30510114, ECO:0000269|PubMed:30926815, CC ECO:0000269|PubMed:34818062, ECO:0000269|PubMed:9294443}. CC -!- MISCELLANEOUS: Present with 1080 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase family. CC PSD-B subfamily. Eukaryotic type I sub-subfamily. {ECO:0000255|HAMAP- CC Rule:MF_03208}. CC -!- CAUTION: Functional localization of the protein to the endoplasmic CC reticulum (ER) has been disputed. ER-localization of the enzyme may be CC difficult to detect in nutrient-rich or respiratory-demanding growth CC conditions. {ECO:0000305|PubMed:33718843, ECO:0000305|PubMed:34818062}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L20973; AAA34918.1; -; Genomic_DNA. DR EMBL; Z71444; CAA96056.1; -; Genomic_DNA. DR EMBL; Z71448; CAA96063.1; -; Genomic_DNA. DR EMBL; X92517; CAA63270.1; -; Genomic_DNA. DR EMBL; BK006947; DAA10379.1; -; Genomic_DNA. DR PIR; A48053; A48053. DR RefSeq; NP_014230.1; NM_001183007.1. DR AlphaFoldDB; P39006; -. DR SMR; P39006; -. DR BioGRID; 35659; 564. DR DIP; DIP-4599N; -. DR FunCoup; P39006; 608. DR IntAct; P39006; 7. DR MINT; P39006; -. DR STRING; 4932.YNL169C; -. DR GlyGen; P39006; 1 site. DR iPTMnet; P39006; -. DR PaxDb; 4932-YNL169C; -. DR PeptideAtlas; P39006; -. DR EnsemblFungi; YNL169C_mRNA; YNL169C; YNL169C. DR GeneID; 855552; -. DR KEGG; sce:YNL169C; -. DR AGR; SGD:S000005113; -. DR SGD; S000005113; PSD1. DR VEuPathDB; FungiDB:YNL169C; -. DR eggNOG; KOG2420; Eukaryota. DR HOGENOM; CLU_029061_1_0_1; -. DR InParanoid; P39006; -. DR OMA; HSPASWV; -. DR OrthoDB; 4330at2759; -. DR BioCyc; YEAST:YNL169C-MONOMER; -. DR BRENDA; 4.1.1.65; 984. DR UniPathway; UPA00558; UER00616. DR BioGRID-ORCS; 855552; 2 hits in 10 CRISPR screens. DR PRO; PR:P39006; -. DR Proteomes; UP000002311; Chromosome XIV. DR RNAct; P39006; protein. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IDA:SGD. DR GO; GO:0140042; P:lipid droplet formation; IDA:SGD. DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IMP:SGD. DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IDA:SGD. DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IMP:UniProtKB. DR GO; GO:0010636; P:positive regulation of mitochondrial fusion; IMP:SGD. DR GO; GO:0010954; P:positive regulation of protein processing; IMP:SGD. DR GO; GO:0016540; P:protein autoprocessing; IDA:SGD. DR HAMAP; MF_03208; PS_decarb_PSD_B_type1_euk; 1. DR InterPro; IPR003817; PS_Dcarbxylase. DR InterPro; IPR033177; PSD-B. DR InterPro; IPR033661; PSD_type1_euk. DR NCBIfam; TIGR00163; PS_decarb; 1. DR PANTHER; PTHR10067; PHOSPHATIDYLSERINE DECARBOXYLASE; 1. DR PANTHER; PTHR10067:SF6; PHOSPHATIDYLSERINE DECARBOXYLASE PROENZYME, MITOCHONDRIAL; 1. DR Pfam; PF02666; PS_Dcarbxylase; 2. PE 1: Evidence at protein level; KW Decarboxylase; Endoplasmic reticulum; Glycoprotein; Lipid biosynthesis; KW Lipid droplet; Lipid metabolism; Lyase; Membrane; Mitochondrion; KW Mitochondrion inner membrane; Phospholipid biosynthesis; KW Phospholipid metabolism; Pyruvate; Reference proteome; Transit peptide; KW Transmembrane; Transmembrane helix; Zymogen. FT TRANSIT 1..48 FT /note="Mitochondrion; not cleaved when targeted to the FT endoplasmic reticulum" FT /evidence="ECO:0000255, ECO:0000305|PubMed:29290583" FT CHAIN 45..500 FT /note="Phosphatidylserine decarboxylase proenzyme 1, FT mitochondrial" FT /id="PRO_0000029843" FT CHAIN 45..462 FT /note="Phosphatidylserine decarboxylase 1 beta chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208" FT /id="PRO_0000029844" FT CHAIN 463..500 FT /note="Phosphatidylserine decarboxylase 1 alpha chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208" FT /id="PRO_0000029845" FT TOPO_DOM 45..79 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208, FT ECO:0000305|PubMed:22984266" FT TRANSMEM 80..98 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208" FT TOPO_DOM 99..500 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208, FT ECO:0000305|PubMed:22984266" FT REGION 57..101 FT /note="Enables targeting to the endoplasmic reticulum in FT addition to mitochondria" FT /evidence="ECO:0000269|PubMed:29290583" FT REGION 475..492 FT /note="Required for processing and stability" FT /evidence="ECO:0000269|PubMed:28473294" FT ACT_SITE 210 FT /note="Charge relay system; for autoendoproteolytic FT cleavage activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208" FT ACT_SITE 348 FT /note="Charge relay system; for autoendoproteolytic FT cleavage activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208" FT ACT_SITE 463 FT /note="Charge relay system; for autoendoproteolytic FT cleavage activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208" FT ACT_SITE 463 FT /note="Schiff-base intermediate with substrate; via pyruvic FT acid; for decarboxylase activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208" FT SITE 462..463 FT /note="Cleavage (non-hydrolytic); by autocatalysis" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208" FT MOD_RES 463 FT /note="Pyruvic acid (Ser); by autocatalysis" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208" FT CARBOHYD 34 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498, FT ECO:0000305|PubMed:29290583" FT MUTAGEN 81..100 FT /note="Missing: In PSD1deltaIM; Mislocalizes to the FT mitochondrial matrix." FT /evidence="ECO:0000269|PubMed:22984266" FT MUTAGEN 189 FT /note="R->A: Impaired processing of the proenzyme." FT /evidence="ECO:0000269|PubMed:33718843" FT MUTAGEN 196 FT /note="R->A: No processing of the proenzyme." FT /evidence="ECO:0000269|PubMed:33718843" FT MUTAGEN 210 FT /note="D->A: No processing of the proenzyme. Increases FT protein localization to the endoplasmic reticulum; when FT associated with A-345 and A-463." FT /evidence="ECO:0000269|PubMed:33718843" FT MUTAGEN 230 FT /note="K->A: Impaired processing of the proenzyme." FT /evidence="ECO:0000269|PubMed:33718843" FT MUTAGEN 345 FT /note="H->A: No processing of the proenzyme. Increases FT protein localization to the endoplasmic reticulum; when FT associated with A-210 and A-463." FT /evidence="ECO:0000269|PubMed:33718843" FT MUTAGEN 346 FT /note="H->A: Impaired processing of the proenzyme." FT /evidence="ECO:0000269|PubMed:33718843" FT MUTAGEN 358 FT /note="R->Q: Changed autocatalytic proteolysis." FT /evidence="ECO:0000269|PubMed:30858161" FT MUTAGEN 385 FT /note="R->A: No processing of the proenzyme." FT /evidence="ECO:0000269|PubMed:33718843" FT MUTAGEN 402..405 FT /note="VGAT->AAAA: No processing of the proenzyme." FT /evidence="ECO:0000269|PubMed:33718843" FT MUTAGEN 407..410 FT /note="VGSI->AAAA: No processing of the proenzyme." FT /evidence="ECO:0000269|PubMed:33718843" FT MUTAGEN 461..463 FT /note="LGS->AAA: No processing of the proenzyme, complete FT loss of activity." FT /evidence="ECO:0000269|PubMed:18644857, FT ECO:0000269|PubMed:33718843" FT MUTAGEN 461 FT /note="L->A: No effect." FT /evidence="ECO:0000269|PubMed:25829489" FT MUTAGEN 462 FT /note="G->A: Significantly impairs processing of the FT proenzyme, retains some activity." FT /evidence="ECO:0000269|PubMed:25829489" FT MUTAGEN 463 FT /note="S->A: No processing of the proenzyme, complete loss FT of activity. Increases protein localization to the FT endoplasmic reticulum; when associated with A-210 and FT A-345." FT /evidence="ECO:0000269|PubMed:22984266, FT ECO:0000269|PubMed:25829489, ECO:0000269|PubMed:28473294, FT ECO:0000269|PubMed:29290583, ECO:0000269|PubMed:33718843" FT MUTAGEN 464 FT /note="T->I: No effect." FT /evidence="ECO:0000269|PubMed:25829489" FT MUTAGEN 475..486 FT /note="Missing: Loss of autocatalytic processing and leads FT to protein degradation. Complete loss of activity. Growth FT on the fermentable carbon source galactose is severely FT decreased." FT /evidence="ECO:0000269|PubMed:28473294" FT MUTAGEN 479..481 FT /note="Missing: Loss of autocatalytic processing and leads FT to protein degradation. Complete loss of activity. Growth FT on the fermentable carbon source galactose is severely FT decreased." FT /evidence="ECO:0000269|PubMed:28473294" FT MUTAGEN 480..486 FT /note="RVGDKVK->AVGDAVA: Impairs processing of the FT proenzyme and increases protein degradation. Decreases FT activity." FT /evidence="ECO:0000269|PubMed:28473294" FT MUTAGEN 480..485 FT /note="Missing: Loss of autocatalytic processing and leads FT to protein degradation. Complete loss of activity. Growth FT on the fermentable carbon source galactose is moderately FT decreased." FT /evidence="ECO:0000269|PubMed:28473294" FT MUTAGEN 482..484 FT /note="Missing: Loss of autocatalytic processing and leads FT to protein degradation. Complete loss of activity. Growth FT on the fermentable carbon source galactose is severely FT decreased." FT /evidence="ECO:0000269|PubMed:28473294" FT MUTAGEN 482 FT /note="G->P: Increases protein degradation." FT /evidence="ECO:0000269|PubMed:28473294" FT MUTAGEN 483..484 FT /note="Missing: Impairs processing of the proenzyme. FT Decreases activity." FT /evidence="ECO:0000269|PubMed:28473294" FT MUTAGEN 486 FT /note="K->A: Impairs processing of the proenzyme and FT increases protein degradation. Decreases activity." FT /evidence="ECO:0000269|PubMed:28473294" FT MUTAGEN 488 FT /note="G->P: Loss of autocatalytic processing and leads to FT protein degradation. Complete loss of activity. Growth on FT the fermentable carbon source galactose is severely FT decreased." FT /evidence="ECO:0000269|PubMed:28473294" FT MUTAGEN 491..492 FT /note="Missing: Increases protein degradation. Decreases FT activity." FT /evidence="ECO:0000269|PubMed:28473294" FT MUTAGEN 492 FT /note="G->P: Increases protein degradation. Decreases FT activity." FT /evidence="ECO:0000269|PubMed:28473294" SQ SEQUENCE 500 AA; 56595 MW; D57047C5AD11777A CRC64; MSIMPVKNAL AQGRTLLMGR MPAVKFSTRM QLRNRTAVLW NRKFSTRLFV QQRRSSGEIV DRAKAAAANS GRKQVSMKWV VLTSFTIVLG TILLVSRNDS TEEDATEGKK GRRTRKIKIF NNNWLFFCYS TLPLNAMSRL WGQVNSLTLP IWVRPWGYRL YSFLFGVNLD EMEDPDLTHY ANLSEFFYRN IKPGTRPVAQ GEDVIASPSD GKILQVGIIN SETGEIEQVK GMTYSIKEFL GTHSHPLMSK SASSLDLTSD EEKHREFARV NRIQLAGSED TEQPLLNFKN EGDQSVREFK PSVSKNIHLL SQLSLNYFSN GFSCSEPHDT ELFFAVIYLA PGDYHHFHSP VDWVCKVRRH FPGDLFSVAP YFQRNFPNLF VLNERVALLG SWKYGFFSMT PVGATNVGSI KLNFDQEFVT NSKSDKHLEP HTCYQAVYEN ASKILGGMPL VKGEEMGGFE LGSTVVLCFE APTEFKFDVR VGDKVKMGQK LGIIGKNDLK //