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Annotation rule MF_00663
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General rule information [?]

Accession MF_00663
Dates 28-JUN-2003 (Created)
18-MAR-2020 (Last updated, Version 22)
Name PS_decarb_PSD_B_type2
Scope
Bacteria
Templates P0A8K1 (PSD_ECOLI); B3L2V1 (PSD_PLAKH): [Recover all]
case <OC:Bacteria>
end case


Propagated annotation [?]


Identifier, protein and gene names [?]

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

Comments [?]

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
Cofactor pyruvate
Note: Binds 1 pyruvoyl group covalently per subunit.
Pathway Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.
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 autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, 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. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase.
Similarity Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Prokaryotic type II sub-subfamily.

Keywords [?]


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 TIGR00163; PS_decarb; 1;

Features [?]

From: PSD_CLOPA (Q46192)
Key     From     To       Description   Tag   Condition   FTGroup
CHAIN     Nter     255       Phosphatidylserine decarboxylase beta chain        
CHAIN     256     Cter       Phosphatidylserine decarboxylase alpha chain        
ACT_SITE     113     113       Charge relay system; for autoendoproteolytic cleavage activity     D  
ACT_SITE     169     169       Charge relay system; for autoendoproteolytic cleavage activity     H  
ACT_SITE     256     256       Charge relay system; for autoendoproteolytic cleavage activity     S  
ACT_SITE     256     256       Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity     S  
SITE     255     256       Cleavage (non-hydrolytic); by autocatalysis     G-S  
MOD_RES     256     256       Pyruvic acid (Ser); by autocatalysis     S  

Additional information [?]

Size range 291-325 amino acids
Related rules MF_00662 (PSD); MF_00664 (PSD)
Fusion 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.