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Annotation rule MF_00664
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General rule information [?]

Accession MF_00664
Dates 28-JUN-2003 (Created)
18-MAR-2020 (Last updated, Version 31)
Name PS_decarb_PSD_A
Scope
Bacteria
Archaea
Templates Q9FDI9 (PSD_RHIME); O28234 (ASD_ARCFU); P0A8K1 (PSD_ECOLI): [Recover all]
Triggered by

Propagated annotation [?]


Identifier, protein and gene names [?]

case <OC:Bacteria>
Identifier
PSD
Protein name
RecName: Full=Phosphatidylserine decarboxylase proenzyme;
EC 4.1.1.65;
Contains:
RecName: Full=Phosphatidylserine decarboxylase alpha chain;
Contains:
RecName: Full=Phosphatidylserine decarboxylase beta chain;
Gene name
psd
else case <OC:Archaea>
Identifier
ASD
Protein name
RecName: Full=Putative archaetidylserine decarboxylase proenzyme;
EC 4.1.1.-;
Contains:
RecName: Full=Archaetidylserine decarboxylase alpha chain;
Contains:
RecName: Full=Archaetidylserine decarboxylase beta chain;
Gene name
asd
end case

Comments [?]

case <OC:Bacteria>
Function Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Catalytic activity RHEA:20828: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
EC 4.1.1.65
Pathway Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.
else case <OC:Archaea>
Function Catalyzes the formation of archaetidylethanolamine (PtdEtn) from archaetidylserine (PtdSer).
Catalytic activity RHEA:51488: archaetidylserine + H(+) = archaetidylethanolamine + CO2
end case
Cofactor pyruvate
Note: Binds 1 pyruvoyl group covalently per subunit.
Subunit Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit.
Subcellular location Cell membrane; Peripheral membrane protein.
Ptm Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain.
Similarity Belongs to the phosphatidylserine decarboxylase family. PSD-A subfamily.

Keywords [?]

Cell membrane
Decarboxylase
Lipid biosynthesis
Lipid metabolism
Lyase
Membrane
Phospholipid biosynthesis
Phospholipid metabolism
Pyruvate
Zymogen

Gene Ontology [?]

GO:0005886; Cellular component: plasma membrane.
GO:0004609; Molecular function: phosphatidylserine decarboxylase activity.
GO:0008654; Biological process: phospholipid biosynthetic process.

Cross-references [?]

Pfam PF02666; PS_Dcarbxylase; 1;
TIGRFAMs TIGR00164; PS_decarb_rel; 1;

Features [?]

case <OC:Bacteria>
From: PSD_RHIME (Q9FDI9)
Key     From     To       Description   Tag   Condition   FTGroup
CHAIN     Nter     189       Phosphatidylserine decarboxylase beta chain        
CHAIN     190     Cter       Phosphatidylserine decarboxylase alpha chain        
else case <OC:Archaea>
CHAIN     Nter     189       Archaetidylserine decarboxylase beta chain        
CHAIN     190     Cter       Archaetidylserine decarboxylase alpha chain        
end case
ACT_SITE     190     190       Schiff-base intermediate with substrate; via pyruvic acid     S  
SITE     189     190       Cleavage (non-hydrolytic); by autocatalysis     G-S  
MOD_RES     190     190       Pyruvic acid (Ser); by autocatalysis     S  

Additional information [?]

Size range 195-265 amino acids
Related rules MF_00662 (PSD); MF_00663 (PSD)
Fusion None
Comments Classification of phosphatidylserine decarboxylase into subfamilies was done according to Daiyasu at al.(2005) (PubMed:16243780).


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