AC   MF_00664;
DC   Protein; auto
TR   HAMAP; MF_00664; -; 1; level=0
XX
Names: PS_decarb_PSD_A
XX
case <OC:Bacteria>
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;
else case <OC:Archaea>
ID   ASD
DE   RecName: Full=Putative archaetidylserine decarboxylase proenzyme;
DE            EC=4.1.1.-;
DE   Contains:
DE     RecName: Full=Archaetidylserine decarboxylase alpha chain;
DE   Contains:
DE     RecName: Full=Archaetidylserine decarboxylase beta chain;
GN   Name=asd;
end case
XX
case <OC:Bacteria>
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   -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC       biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step
CC       2/2.
else case <OC:Archaea>
CC   -!- FUNCTION: Catalyzes the formation of archaetidylethanolamine (PtdEtn)
CC       from archaetidylserine (PtdSer).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=archaetidylserine + H(+) = archaetidylethanolamine + CO2;
CC         Xref=Rhea:RHEA:51488, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:71517, ChEBI:CHEBI:134176;
end case
CC   -!- COFACTOR:
CC       Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC       Note=Binds 1 pyruvoyl group covalently per subunit.;
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 post-translation
CC       cleavage follows an unusual pathway, termed non-hydrolytic serinolysis,
CC       in which the side chain hydroxyl group of the serine supplies its
CC       oxygen atom to form the C-terminus of the beta chain, while the
CC       remainder of the serine residue undergoes an oxidative deamination to
CC       produce ammonia and the pyruvoyl prosthetic group on the alpha chain.
CC   -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase family.
CC       PSD-A subfamily.
XX
DR   Pfam; PF02666; PS_Dcarbxylase; 1; trigger=no
DR   NCBIfam; TIGR00164; PS_decarb_rel; 1; trigger=no
XX
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
XX
GO   GO:0005886; C:plasma membrane
GO   GO:0004609; F:phosphatidylserine decarboxylase activity
GO   GO:0008654; P:phospholipid biosynthetic process
XX
FT   From: PSD_RHIME (Q9FDI9)
case <OC:Bacteria>
FT   CHAIN           Nter..189
FT                   /note="Phosphatidylserine decarboxylase beta chain"
FT   CHAIN           190..Cter
FT                   /note="Phosphatidylserine decarboxylase alpha chain"
else case <OC:Archaea>
FT   CHAIN           Nter..189
FT                   /note="Archaetidylserine decarboxylase beta chain"
FT   CHAIN           190..Cter
FT                   /note="Archaetidylserine decarboxylase alpha chain"
end case
FT   ACT_SITE        190
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid"
FT   Condition: S
FT   SITE            189..190
FT                   /note="Cleavage (non-hydrolytic); by autocatalysis"
FT   Condition: G-S
FT   MOD_RES         190
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT   Condition: S
XX
Size: 195-265;
Related: MF_00662; MF_00663;
Template: Q9FDI9; O28234; P0A8K1;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: in RUEPO, RUEST
Comments: Classification of phosphatidylserine decarboxylase into subfamilies
 was done according to Daiyasu at al.(2005) (PubMed:16243780).
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# Revision 1.32 2023/06/01
//