Q1GMQ8 · PSD_RUEST
- ProteinPhosphatidylserine decarboxylase proenzyme
- Genepsd
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids233 (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 | 187-188 | Cleavage (non-hydrolytic); by autocatalysis | ||||
Sequence: GS | ||||||
Active site | 188 | Schiff-base intermediate with substrate; via pyruvic acid | ||||
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
Encoded on
- Plasmid megaplasmid TM1040
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Rhodobacterales > Roseobacteraceae > Ruegeria
Accessions
- Primary accessionQ1GMQ8
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_0000262271 | 1-187 | Phosphatidylserine decarboxylase beta chain | |||
Sequence: MNMIGTFIKPMHPEGRKFVAIFAAVTFGLFLLTPILGWIGVGLTVWCYYFFRDPERVTPARPGLVISPADGVVSLIEPAVPPAELGLPDVPLTRVSVFMSVFNCHVNRAPVAGEVTAVAYRPGKFFNASLDKASADNERNSLAIRMEDGRDLAVVQIAGLVARRIVCFVKPGAQLGRGERFGLIRFG | ||||||
Modified residue | 188 | Pyruvic acid (Ser); by autocatalysis | ||||
Sequence: S | ||||||
Chain | PRO_0000262272 | 188-233 | Phosphatidylserine decarboxylase alpha chain | |||
Sequence: SRLDVYLPEGVSPQVEIGQTMIAGETVIAELGTGVHTDQNKGELHG |
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.
Structure
Family & Domains
Sequence similarities
Belongs to the phosphatidylserine decarboxylase family. PSD-A subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length233
- Mass (Da)25,160
- Last updated2006-06-27 v1
- Checksum0FFE968DED39D494
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000376 EMBL· GenBank· DDBJ | ABF62058.1 EMBL· GenBank· DDBJ | Genomic DNA |