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HAMAP rule MF_00664

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General rule information [?]

Accession MF_00664
Dates 28-JUN-2003 (Created)
2-FEB-2024 (Last updated, Version 33)
Name PS_decarb_PSD_A
Scope(s) Bacteria
Template(s) Q9FDI9 (PSD_RHIME); O28234 (ASD_ARCFU); P0A8K1 (PSD_ECOLI); [ Recover all ]
Triggered by HAMAP; MF_00664 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

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

Comments [?]

case <OC:Bacteria>
FUNCTIONCatalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
CATALYTIC ACTIVITY Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2- diacyl-sn-glycero-3-phosphoethanolamine + CO2; Xref=Rhea:RHEA:20828, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57262, ChEBI:CHEBI:64612; EC=;
PATHWAYPhospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.
else case <OC:Archaea>
FUNCTIONCatalyzes the formation of archaetidylethanolamine (PtdEtn) from archaetidylserine (PtdSer).
CATALYTIC ACTIVITY Reaction=archaetidylserine + H(+) = archaetidylethanolamine + CO2; Xref=Rhea:RHEA:51488, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:71517, ChEBI:CHEBI:134176;
end case
COFACTOR Name=pyruvate; Xref=ChEBI:CHEBI:15361; Note=Binds 1 pyruvoyl group covalently per subunit.;
SUBUNITHeterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit.
SUBCELLULAR LOCATIONCell membrane; Peripheral membrane protein.
PTMIs 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.
SIMILARITYBelongs to the phosphatidylserine decarboxylase family. PSD-A subfamily.

Keywords [?]

Gene Ontology [?]

GO:0005886; Cellular component:plasma membrane
case <OCellular component:Bacteria>
GO:0004609; Molecular function:phosphatidylserine decarboxylase activity
GO:0006646; Biological process:phosphatidylethanolamine biosynthetic process
else case <OCellular component:Archaea>
GO:0008654; Biological process:phospholipid biosynthetic process
end case

Cross-references [?]

Pfam PF02666; PS_Dcarbxylase; 1;
NCBIfam TIGR00164; PS_decarb_rel; 1;

Features [?]

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

Additional information [?]

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

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