HAMAP rule MF_00663
General rule information
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| Accession | MF_00663 |
| Dates | 28-JUN-2003 (Created)
1-JUN-2023 (Last updated, Version 23) |
| Name | PS_decarb_PSD_B_type2 |
| Scope(s) |
Bacteria |
| Template(s) | P0A8K1 (PSD_ECOLI); B3L2V1 (PSD_PLAKH); [ Recover all ] |
| Triggered by |
case c? <OC:Bacteria>
HAMAP; MF_00663 (Get profile general information and statistics) end case
|
Propagated annotation
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Identifier, protein and gene names
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| 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 | Name=psd; |
Comments
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| FUNCTION | Catalyzes 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=4.1.1.65; |
| COFACTOR | Name=pyruvate; Xref=ChEBI:CHEBI:15361; 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
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| Cell membrane |
| Decarboxylase |
| Lipid biosynthesis |
| Lipid metabolism |
| Lyase |
| Membrane |
| Phospholipid biosynthesis |
| Phospholipid metabolism |
| Pyruvate |
| Zymogen |
Gene Ontology
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| GO:0005886; Cellular component:plasma membrane |
| GO:0004609; Molecular function:phosphatidylserine decarboxylase activity |
| GO:0008654; Biological process:phospholipid biosynthetic process |
Cross-references
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Features
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| From: PSD_CLOPA (Q46192) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| CHAIN | Nter | 255 | /note="Phosphatidylserine decarboxylase beta chain" | |||||||||
| CHAIN | 256 | Cter | /note="Phosphatidylserine decarboxylase alpha chain" | |||||||||
| ACT_SITE | 113 | 113 | /note="Charge relay system; for autoendoproteolytic cleavage activity" | D | ||||||||
| ACT_SITE | 169 | 169 | /note="Charge relay system; for autoendoproteolytic cleavage activity" | H | ||||||||
| ACT_SITE | 256 | 256 | /note="Charge relay system; for autoendoproteolytic cleavage activity" | S | ||||||||
| ACT_SITE | 256 | 256 | /note="Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity" | S | ||||||||
| SITE | 255 | 256 | /note="Cleavage (non-hydrolytic); by autocatalysis" | G-S | ||||||||
| MOD_RES | 256 | 256 | /note="Pyruvic acid (Ser); by autocatalysis" | S | ||||||||
Additional information
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| Size range | 291-325 amino acids |
| Related rules |
MF_00662 MF_00664 |
| Fusion | Nter: None 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. |