B3ESH0 · PSD_AMOA5
- ProteinPhosphatidylserine decarboxylase proenzyme
- Genepsd
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids225 (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 site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Site | 188-189 | Cleavage (non-hydrolytic); by autocatalysis | |||
Active site | 189 | Schiff-base intermediate with substrate; via pyruvic acid | |||
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 > Bacteroidota > Cytophagia > Cytophagales > Amoebophilaceae > Candidatus Amoebophilus
Accessions
- Primary accessionB3ESH0
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_1000192890 | 1-188 | Phosphatidylserine decarboxylase beta chain | ||
Modified residue | 189 | Pyruvic acid (Ser); by autocatalysis | |||
Chain | PRO_1000192891 | 189-225 | Phosphatidylserine decarboxylase alpha chain | ||
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 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.
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-A subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length225
- Mass (Da)25,629
- Last updated2008-07-22 v1
- Checksum20EF2DC5A4AF5F53
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP001102 EMBL· GenBank· DDBJ | ACE06172.1 EMBL· GenBank· DDBJ | Genomic DNA |