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HAMAP rule MF_00662

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General rule information [?]

Accession MF_00662
Dates 28-JUN-2003 (Created)
2-FEB-2024 (Last updated, Version 30)
Name PS_decarb_PSD_B_type1
Scope(s) Bacteria
Template(s) P0A8K1 (PSD_ECOLI); P39822 (PSD_BACSU); [ Recover all ]
Triggered by HAMAP; MF_00662 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

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;

Comments [?]

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=;
COFACTOR Name=pyruvate; Xref=ChEBI:CHEBI:15361; Note=Binds 1 pyruvoyl group covalently per subunit.;
PATHWAYPhospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.
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 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.
SIMILARITYBelongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Prokaryotic type I sub-subfamily.

Keywords [?]

Gene Ontology [?]

GO:0005886; Cellular component:plasma membrane
GO:0004609; Molecular function:phosphatidylserine decarboxylase activity
GO:0006646; Biological process:phosphatidylethanolamine biosynthetic process

Cross-references [?]

Pfam PF02666; PS_Dcarbxylase; 1;
NCBIfam TIGR00163; PS_decarb; 1;

Features [?]

From: PSD_ECOLI (P0A8K1)
Key From To Description Tag Condition FTGroup
CHAIN Nter 253 /note="Phosphatidylserine decarboxylase beta chain"
CHAIN 254 Cter /note="Phosphatidylserine decarboxylase alpha chain"
ACT_SITE 90 90 /note="Charge relay system; for autoendoproteolytic cleavage activity" D
ACT_SITE 147 147 /note="Charge relay system; for autoendoproteolytic cleavage activity" H
ACT_SITE 254 254 /note="Charge relay system; for autoendoproteolytic cleavage activity" S
ACT_SITE 254 254 /note="Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity" S
SITE 253 254 /note="Cleavage (non-hydrolytic); by autocatalysis" G-S
MOD_RES 254 254 /note="Pyruvic acid (Ser); by autocatalysis" S

Additional information [?]

Size range 259-341 amino acids
Related rules MF_00663
Fusion Nter: <Unknown>; <Rhodanese domains> Cter: 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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