A1VUQ1 · PSD_POLNA
- ProteinPhosphatidylserine decarboxylase proenzyme
- Genepsd
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids289 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Catalytic activity
- a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H+ = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
Cofactor
Note: Binds 1 pyruvoyl group covalently per subunit.
Pathway
Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.
Features
Showing features for active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 88 | Charge relay system; for autoendoproteolytic cleavage activity | ||||
Sequence: D | ||||||
Active site | 145 | Charge relay system; for autoendoproteolytic cleavage activity | ||||
Sequence: H | ||||||
Site | 250-251 | Cleavage (non-hydrolytic); by autocatalysis | ||||
Sequence: GS | ||||||
Active site | 251 | Charge relay system; for autoendoproteolytic cleavage activity | ||||
Sequence: S | ||||||
Active site | 251 | Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | phosphatidylserine decarboxylase activity | |
Biological Process | phosphatidylethanolamine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphatidylserine decarboxylase proenzyme
- EC number
- Cleaved into 2 chains
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Comamonadaceae > Polaromonas
Accessions
- Primary accessionA1VUQ1
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000026562 | 1-250 | Phosphatidylserine decarboxylase beta chain | |||
Sequence: MSDRLAVLPQYLLPKQALTHFAGFVASRERGWVTTEIIRRFVAKYRVNMSEALDSDIASYLTFNDFFTRALKPGARPLAQAALVCPVDGAISQFGAIEHDQIFQAKGHHYSTTALVGGDAALAAHYQNGHFATIYLSPKDYHRIHMPCDGRLTRMIYVPGDLFSVNPVTARGVPGLFARNERVVCVFESARGPFVLALVGATIVGSMATVWHGVVNPPRGKAVREWRYPASGQPEVVLRQGEEMGRFLLG | ||||||
Modified residue | 251 | Pyruvic acid (Ser); by autocatalysis | ||||
Sequence: S | ||||||
Chain | PRO_1000026563 | 251-289 | Phosphatidylserine decarboxylase alpha chain | |||
Sequence: STVVLLFPKGPLRFNPDWEPGRAVRLGEAMADVAADSQR |
Post-translational modification
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.
Keywords
- PTM
Interaction
Subunit
Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit.
Protein-protein interaction databases
Structure
Family & Domains
Sequence similarities
Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Prokaryotic type I sub-subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length289
- Mass (Da)31,778
- Last updated2007-02-06 v1
- Checksum747F000D5EBED966
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000529 EMBL· GenBank· DDBJ | ABM39379.1 EMBL· GenBank· DDBJ | Genomic DNA |