AC   MF_03209;
DC   Protein; auto
c?   <OC:Eukaryota>
TR   HAMAP; MF_00663; -; 1; level=0
XX
Names: PS_decarb_PSD_B_type2_euk
XX
ID   PSD2
DE   RecName: Full=Phosphatidylserine decarboxylase proenzyme 2;
DE            EC=4.1.1.65;
DE   Contains:
DE     RecName: Full=Phosphatidylserine decarboxylase 2 beta chain;
DE   Contains:
DE     RecName: Full=Phosphatidylserine decarboxylase 2 alpha chain;
GN   Name=PSD2;
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
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC       biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step
CC       2/2.
case <OC:Ascomycota>
CC   -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit and a
CC       small pyruvoyl-containing alpha subunit. Interacts with pstB2. This
CC       interaction may be a means to structurally tether the donor membrane
CC       (ER) harboring PstB2 to acceptor membranes (Golgi/endosomes) harboring
CC       PSD2 during PtdSer transport to the site of PtdEtn synthesis.
else
CC   -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit and a
CC       small pyruvoyl-containing alpha subunit.
end case
case <OC:Fungi>
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane
CC       protein; Cytoplasmic side. Endosome membrane; Peripheral membrane
CC       protein; Cytoplasmic side.
end case
case <Feature:PS50004> and <OC:Saccharomycetales>
CC   -!- DOMAIN: The C2 domains have an essential, but non-catalytic function.
CC       They may facilitate interaction with PstB2 and are required for lipid
CC       transport function.
else case <Feature:PS50004>
CC   -!- DOMAIN: The C2 domains have an essential, but non-catalytic function.
CC       They may facilitate interactions with other proteins and are required
CC       for lipid transport function.
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 II sub-subfamily.
XX
DR   PROSITE; PS50004; C2; 1-2; trigger=yes
DR   PROSITE; PS00018; EF_HAND_1; 0-2; trigger=no
DR   PROSITE; PS50222; EF_HAND_2; 0-2; trigger=yes
DR   Pfam; PF00168; C2; 1-2; trigger=no
DR   Pfam; PF02666; PS_Dcarbxylase; 1; trigger=no
DR   Pfam; PF13499; EF-hand_7; 0-1; trigger=no
DR   NCBIfam; TIGR00163; PS_decarb; 1; trigger=no
XX
KW   Decarboxylase
case <OC:Fungi>
KW   Endosome
KW   Golgi apparatus
end case
KW   Lipid biosynthesis
KW   Lipid metabolism
KW   Lyase
KW   Membrane
KW   Phospholipid biosynthesis
KW   Phospholipid metabolism
KW   Pyruvate
KW   Zymogen
XX
case <OC:Fungi>
GO   GO:0005768; C:endosome
GO   GO:0005795; C:Golgi stack
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: PSD2_YEAST (P53037)
FT   CHAIN           Nter..1042
FT                   /note="Phosphatidylserine decarboxylase 2 beta chain"
FT   CHAIN           1043..Cter
FT                   /note="Phosphatidylserine decarboxylase 2 alpha chain"
FT   ACT_SITE        899
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT   Condition: D
FT   ACT_SITE        956
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT   Condition: H
FT   ACT_SITE        1043
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT   Condition: S
FT   ACT_SITE        1043
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid; for decarboxylase activity"
FT   Condition: S
FT   SITE            1042..1043
FT                   /note="Cleavage (non-hydrolytic); by autocatalysis"
FT   Condition: G-S
FT   MOD_RES         1043
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT   Condition: S
XX
Size: 383-1400;
Related: None;
Template: P53037;
Scope:
 Eukaryota
Fusion:
 Nter: None
 Cter: None
Duplicate: in ARATH
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 1.6 2023/06/01
//