O14111 · PSD3_SCHPO
- ProteinPhosphatidylserine decarboxylase proenzyme 3
- Genepsd3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids967 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine (By similarity).
Together with psd1 and psd2, responsible for the majority of phosphatidylethanolamine synthesis (PubMed:19286980).
Together with psd1 and psd2, responsible for the majority of phosphatidylethanolamine synthesis (PubMed:19286980).
Catalytic activity
- a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H+ = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 pyruvoyl group covalently per subunit.
Pathway
Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 343 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 346 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 349 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 769 | Charge relay system; for autoendoproteolytic cleavage activity | ||||
Sequence: D | ||||||
Active site | 825 | Charge relay system; for autoendoproteolytic cleavage activity | ||||
Sequence: H | ||||||
Site | 911-912 | Cleavage (non-hydrolytic); by autocatalysis | ||||
Sequence: GS | ||||||
Active site | 912 | Charge relay system; for autoendoproteolytic cleavage activity | ||||
Sequence: S | ||||||
Active site | 912 | Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cell division site | |
Cellular Component | cytosol | |
Cellular Component | endosome membrane | |
Cellular Component | fungal-type vacuole membrane | |
Cellular Component | Golgi membrane | |
Cellular Component | Golgi stack | |
Molecular Function | metal ion binding | |
Molecular Function | phosphatidylserine decarboxylase activity | |
Molecular Function | phospholipid binding | |
Biological Process | phosphatidylcholine biosynthetic process | |
Biological Process | phosphatidylethanolamine biosynthetic process | |
Biological Process | protein autoprocessing |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphatidylserine decarboxylase proenzyme 3
- EC number
- Cleaved into 2 chains
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Taphrinomycotina > Schizosaccharomycetes > Schizosaccharomycetales > Schizosaccharomycetaceae > Schizosaccharomyces
Accessions
- Primary accessionO14111
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Golgi apparatus membrane ; Peripheral membrane protein
Endosome membrane ; Peripheral membrane protein
Note: Localizes at the barrier septum.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000416837 | 1-911 | Phosphatidylserine decarboxylase 3 beta chain | |||
Sequence: MPFTKSCRSANTLRKGIKNGKLILKIIVNDIDNVESCLSGDESNDSKKSSASFYMKLKYGSYRALADNILSTDENRKEDIAVFDVPLPNGLQIDTFTLCLYRKSKWKKQIVGEAYIGIQALLLSTNPDETCKYPVISPPSGRNKENQSPSHQICNLSLKWIIYDPEDADADSKTLAKAWLQQIKMNQTSIDPMSNISKSLKELEVDNVESDLEDSSFIAEPDSSIPPSESSVSISTDTGKETPPSKSKKSSNQPYVSIGEGNSDLLGFVFLEIISVSNLPPLKNVFRTGFDMDPFVITAFSKNIFRTKWLRHNLNPVYNEKFLFEVGAFESNYDLVFKVVDHDKMSLNDSIAVGSFNVQSIINSSAQVDPETGLYSFNIETSSPSQDTSSKAEDSPTVQKIADDFSSAVGKDLRTDIIEQIIPLTLCCKHDFSTPRDVKLSFKAMFFPIAALRQKFWRVMLAQYGDIEDGHIGKLGMYAVLDTLGSNIPNSMVDDIYTELSSKNHDDTSDSITVDEAVICLERLVDLVCHQDQQATQTPQSPSSNEESGPGTPTQTSDQYEDSEDSRNFPSKLYLVYLSNCPLCLKFKLSKVNQQKATVHLATCASHDWKRVDRLMMTSYVSLNQAQRRWFSKAFAKVVYGSSKVGSTSATTLVQNRQTGQIQEEKMNAYVRIGIRLLYRGIRNRRIEGSKVKKILRSLTLKQGMKYDSPISVKEIKPFIRFFDLNMNEVDMPVGGFKTFNEFFYRKLKPGSRPCAFPDNPDILVSPADSRIVAYECIEKATTYWIKGTEFTVERLLGYSNEAQRFVGGSICISRLAPQDYHRFHSPVNGCIGPITKIEGQYYTVNPMAIRSYLDVFGENVRVLIPIDSNEFGKVMLVAVGAMMVGSTVLTVDEGKIVQRSDELGYFKFGG | ||||||
Chain | PRO_0000303954 | 1-967 | Phosphatidylserine decarboxylase proenzyme 3 | |||
Sequence: MPFTKSCRSANTLRKGIKNGKLILKIIVNDIDNVESCLSGDESNDSKKSSASFYMKLKYGSYRALADNILSTDENRKEDIAVFDVPLPNGLQIDTFTLCLYRKSKWKKQIVGEAYIGIQALLLSTNPDETCKYPVISPPSGRNKENQSPSHQICNLSLKWIIYDPEDADADSKTLAKAWLQQIKMNQTSIDPMSNISKSLKELEVDNVESDLEDSSFIAEPDSSIPPSESSVSISTDTGKETPPSKSKKSSNQPYVSIGEGNSDLLGFVFLEIISVSNLPPLKNVFRTGFDMDPFVITAFSKNIFRTKWLRHNLNPVYNEKFLFEVGAFESNYDLVFKVVDHDKMSLNDSIAVGSFNVQSIINSSAQVDPETGLYSFNIETSSPSQDTSSKAEDSPTVQKIADDFSSAVGKDLRTDIIEQIIPLTLCCKHDFSTPRDVKLSFKAMFFPIAALRQKFWRVMLAQYGDIEDGHIGKLGMYAVLDTLGSNIPNSMVDDIYTELSSKNHDDTSDSITVDEAVICLERLVDLVCHQDQQATQTPQSPSSNEESGPGTPTQTSDQYEDSEDSRNFPSKLYLVYLSNCPLCLKFKLSKVNQQKATVHLATCASHDWKRVDRLMMTSYVSLNQAQRRWFSKAFAKVVYGSSKVGSTSATTLVQNRQTGQIQEEKMNAYVRIGIRLLYRGIRNRRIEGSKVKKILRSLTLKQGMKYDSPISVKEIKPFIRFFDLNMNEVDMPVGGFKTFNEFFYRKLKPGSRPCAFPDNPDILVSPADSRIVAYECIEKATTYWIKGTEFTVERLLGYSNEAQRFVGGSICISRLAPQDYHRFHSPVNGCIGPITKIEGQYYTVNPMAIRSYLDVFGENVRVLIPIDSNEFGKVMLVAVGAMMVGSTVLTVDEGKIVQRSDELGYFKFGGSTVITLFEPNVTSFDEDLLRNSKTKIETLVKMGERIGQKIDPNKPTDAEDHSKSDS | ||||||
Modified residue | 912 | Pyruvic acid (Ser); by autocatalysis | ||||
Sequence: S | ||||||
Chain | PRO_0000416838 | 912-967 | Phosphatidylserine decarboxylase 3 alpha chain | |||
Sequence: STVITLFEPNVTSFDEDLLRNSKTKIETLVKMGERIGQKIDPNKPTDAEDHSKSDS |
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
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 217-255 | Disordered | ||||
Sequence: FIAEPDSSIPPSESSVSISTDTGKETPPSKSKKSSNQPY | ||||||
Compositional bias | 221-255 | Polar residues | ||||
Sequence: PDSSIPPSESSVSISTDTGKETPPSKSKKSSNQPY | ||||||
Domain | 250-373 | C2 | ||||
Sequence: SSNQPYVSIGEGNSDLLGFVFLEIISVSNLPPLKNVFRTGFDMDPFVITAFSKNIFRTKWLRHNLNPVYNEKFLFEVGAFESNYDLVFKVVDHDKMSLNDSIAVGSFNVQSIINSSAQVDPETG | ||||||
Compositional bias | 532-559 | Polar residues | ||||
Sequence: DQQATQTPQSPSSNEESGPGTPTQTSDQ | ||||||
Region | 532-566 | Disordered | ||||
Sequence: DQQATQTPQSPSSNEESGPGTPTQTSDQYEDSEDS | ||||||
Region | 947-967 | Disordered | ||||
Sequence: IGQKIDPNKPTDAEDHSKSDS |
Domain
The C2 domains have an essential, but non-catalytic function. They may facilitate interactions with other proteins and are required for lipid transport function.
Sequence similarities
Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Eukaryotic type II sub-subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length967
- Mass (Da)108,213
- Last updated2012-04-18 v2
- Checksum5B2115FB91FA42BC
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 221-255 | Polar residues | ||||
Sequence: PDSSIPPSESSVSISTDTGKETPPSKSKKSSNQPY | ||||||
Compositional bias | 532-559 | Polar residues | ||||
Sequence: DQQATQTPQSPSSNEESGPGTPTQTSDQ |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CU329670 EMBL· GenBank· DDBJ | CAB11699.2 EMBL· GenBank· DDBJ | Genomic DNA |