AC   MF_00662;
DC   Protein; auto
TR   HAMAP; MF_00662; -; 1; level=0
XX
Names: PS_decarb_PSD_B_type1
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ID   PSD
DE   RecName: Full=Phosphatidylserine decarboxylase proenzyme;
DE            EC=4.1.1.65;
DE   Contains:
DE     RecName: Full=Phosphatidylserine decarboxylase alpha chain;
DE   Contains:
DE     RecName: Full=Phosphatidylserine decarboxylase beta chain;
GN   Name=psd;
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CC   -!- FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn)
CC       from phosphatidylserine (PtdSer).
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.
CC   -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit and a
CC       small pyruvoyl-containing alpha subunit.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
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. Prokaryotic type I sub-subfamily.
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DR   Pfam; PF02666; PS_Dcarbxylase; 1; trigger=no
DR   NCBIfam; TIGR00163; PS_decarb; 1; trigger=no
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KW   Cell membrane
KW   Decarboxylase
KW   Lipid biosynthesis
KW   Lipid metabolism
KW   Lyase
KW   Membrane
KW   Phospholipid biosynthesis
KW   Phospholipid metabolism
KW   Pyruvate
KW   Zymogen
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GO   GO:0005886; C:plasma membrane
GO   GO:0004609; F:phosphatidylserine decarboxylase activity
GO   GO:0008654; P:phospholipid biosynthetic process
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FT   From: PSD_ECOLI (P0A8K1)
FT   CHAIN           Nter..253
FT                   /note="Phosphatidylserine decarboxylase beta chain"
FT   CHAIN           254..Cter
FT                   /note="Phosphatidylserine decarboxylase alpha chain"
FT   ACT_SITE        90
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT   Condition: D
FT   ACT_SITE        147
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT   Condition: H
FT   ACT_SITE        254
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT   Condition: S
FT   ACT_SITE        254
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid; for decarboxylase activity"
FT   Condition: S
FT   SITE            253..254
FT                   /note="Cleavage (non-hydrolytic); by autocatalysis"
FT   Condition: G-S
FT   MOD_RES         254
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT   Condition: S
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Size: 259-341;
Related: MF_00663; MF_00664;
Template: P0A8K1; P39822;
Scope:
 Bacteria
Fusion:
 Nter: <Unknown>; <Rhodanese domains>
 Cter: None
Duplicate: None
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.
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# Revision 1.29 2023/06/01
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