AC MF_03208; DC Protein; auto TR HAMAP; MF_03208; -; 1; level=0 XX Names: PS_decarb_PSD_B_type1_euk XX case ID PSD DE RecName: Full=Phosphatidylserine decarboxylase proenzyme; DE EC=4.1.1.65; DE Contains: DE RecName: Full=Phosphatidylserine decarboxylase beta chain; DE Contains: DE RecName: Full=Phosphatidylserine decarboxylase alpha chain; DE Flags: Precursor; else case or ID PSD1 DE RecName: Full=Phosphatidylserine decarboxylase proenzyme 1, mitochondrial; DE EC=4.1.1.65; DE Contains: DE RecName: Full=Phosphatidylserine decarboxylase 1 beta chain; DE Contains: DE RecName: Full=Phosphatidylserine decarboxylase 1 alpha chain; DE Flags: Precursor; else ID PISD DE RecName: Full=Phosphatidylserine decarboxylase proenzyme, mitochondrial; DE EC=4.1.1.65; DE Contains: DE RecName: Full=Phosphatidylserine decarboxylase beta chain; DE Contains: DE RecName: Full=Phosphatidylserine decarboxylase alpha chain; DE Flags: Precursor; end case case GN Name=PISD; else case GN Name=psd-1; else case GN Name=PSD1; end case XX 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 -!- 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; CC -!- COFACTOR: CC Name=pyruvate; Xref=ChEBI:CHEBI:15361; CC Note=Binds 1 pyruvoyl group covalently per subunit.; case not CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine CC biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step CC 2/2. end case CC -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit and a CC small pyruvoyl-containing alpha subunit. case CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass CC membrane protein. Note=Equally found in the membrane-bound as well as CC in the soluble fraction. else case ( or ) CC -!- SUBCELLULAR LOCATION: Phosphatidylserine decarboxylase 1 beta chain: CC Mitochondrion inner membrane; Single-pass membrane protein; CC Intermembrane side. CC -!- SUBCELLULAR LOCATION: Phosphatidylserine decarboxylase 1 alpha chain: CC Mitochondrion inner membrane; Peripheral membrane protein; CC Intermembrane side. Note=Anchored to the mitochondrial inner membrane CC through its interaction with the integral membrane beta chain. else CC -!- SUBCELLULAR LOCATION: Phosphatidylserine decarboxylase beta chain: CC Mitochondrion inner membrane; Single-pass membrane protein; CC Intermembrane side. CC -!- SUBCELLULAR LOCATION: Phosphatidylserine decarboxylase alpha chain: CC Mitochondrion inner membrane; Peripheral membrane protein; CC Intermembrane side. Note=Anchored to the mitochondrial inner membrane CC through its interaction with the integral membrane beta chain. end case 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. The autoendoproteolytic CC cleavage occurs by a canonical serine protease mechanism, in which the CC side chain hydroxyl group of the serine supplies its oxygen atom to CC form the C-terminus of the beta chain, while the remainder of the CC serine residue undergoes an oxidative deamination to produce ammonia CC and the pyruvoyl prosthetic group on the alpha chain. During this CC reaction, the Ser that is part of the protease active site of the CC proenzyme becomes the pyruvoyl prosthetic group, which constitutes an CC essential element of the active site of the mature decarboxylase. CC -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase family. CC PSD-B subfamily. Eukaryotic type I sub-subfamily. case not and not CC -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal CC transit peptide but none has been predicted. end case XX DR Pfam; PF02666; PS_Dcarbxylase; 1; trigger=no DR NCBIfam; TIGR00163; PS_decarb; 1; trigger=no case not DR General; TransitM; -; 0-1; trigger=yes end case XX KW Decarboxylase KW Lipid biosynthesis KW Lipid metabolism KW Lyase KW Membrane KW Transmembrane KW Transmembrane helix case KW Endoplasmic reticulum else KW Mitochondrion KW Mitochondrion inner membrane end case KW Phospholipid biosynthesis KW Phospholipid metabolism KW Pyruvate KW Zymogen XX case GO GO:0005789; C:endoplasmic reticulum membrane else GO GO:0005743; C:mitochondrial inner membrane end case GO GO:0004609; F:phosphatidylserine decarboxylase activity GO GO:0006646; P:phosphatidylethanolamine biosynthetic process GO GO:0016540; P:protein autoprocessing XX FT From: PSD_PLAKH (B3L2V1) case or FT CHAIN Nter..307 FT /note="Phosphatidylserine decarboxylase 1 beta chain" FT CHAIN 308..Cter FT /note="Phosphatidylserine decarboxylase 1 alpha chain" else FT CHAIN Nter..307 FT /note="Phosphatidylserine decarboxylase beta chain" FT CHAIN 308..Cter FT /note="Phosphatidylserine decarboxylase alpha chain" end case FT TRANSMEM 18..36 FT /note="Helical" case not FT TOPO_DOM Nter..17 FT /note="Mitochondrial matrix" FT TOPO_DOM 37..Cter FT /note="Mitochondrial intermembrane" end case FT ACT_SITE 139 FT /note="Charge relay system; for autoendoproteolytic FT cleavage activity" FT Condition: D FT ACT_SITE 198 FT /note="Charge relay system; for autoendoproteolytic FT cleavage activity" FT Condition: H FT ACT_SITE 308 FT /note="Charge relay system; for autoendoproteolytic FT cleavage activity" FT Condition: S FT ACT_SITE 308 FT /note="Schiff-base intermediate with substrate; via pyruvic FT acid; for decarboxylase activity" FT Condition: S FT SITE 307..308 FT /note="Cleavage (non-hydrolytic); by autocatalysis" FT Condition: G-S FT MOD_RES 308 FT /note="Pyruvic acid (Ser); by autocatalysis" FT Condition: S XX Size: 336-655; Related: None; Template: B3L2V1; P39006; Scope: Eukaryota Fusion: Nter: None Cter: None Duplicate: in SCHPO Plasmid: None Comments: Classification of phosphatidylserine decarboxylase into subfamilies was done according to Daiyasu at al.(2005) (PubMed:16243780) for PSD-A and PSD-B and Voelker D.R.(1997) (PubMed:9370338) for type I and type II. XX # Revision 1.8 2023/06/01 //