D3ZAW2 · PISD_RAT
- ProteinPhosphatidylserine decarboxylase proenzyme, mitochondrial
- GenePisd
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids406 (go to sequence)
- Protein existenceEvidence at protein level
- 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. May be involved in lipid droplet biogenesis at the endoplasmic reticulum membrane (By similarity).
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.
Activity regulation
Inhibited by hydroxylamine.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
67 μM | phosphatidylserine |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
77 nmol/h/mg |
pH Dependence
Optimum pH is 5.
Pathway
Phospholipid metabolism; phosphatidylethanolamine biosynthesis.
Features
Showing features for active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 188 | Charge relay system; for autoendoproteolytic cleavage activity | ||||
Sequence: D | ||||||
Active site | 264 | Charge relay system; for autoendoproteolytic cleavage activity | ||||
Sequence: H | ||||||
Site | 374-375 | Cleavage (non-hydrolytic); by autocatalysis | ||||
Sequence: GS | ||||||
Active site | 375 | Charge relay system; for autoendoproteolytic cleavage activity | ||||
Sequence: S | ||||||
Active site | 375 | Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | lipid droplet | |
Cellular Component | mitochondrial inner membrane | |
Cellular Component | mitochondrion | |
Molecular Function | phosphatidylserine decarboxylase activity | |
Biological Process | lipid droplet formation | |
Biological Process | mitochondrial protein catabolic process | |
Biological Process | phosphatidylethanolamine biosynthetic process | |
Biological Process | protein autoprocessing | |
Biological Process | regulation of mitochondrion organization |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphatidylserine decarboxylase proenzyme, mitochondrial
- EC number
- Cleaved into 2 chains
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionD3ZAW2
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Predominantly localizes to lipid droplets in lipid-replete conditions, and to mitochondria in lipid-deplete conditions.
Phosphatidylserine decarboxylase beta chain
Mitochondrion inner membrane ; Single-pass membrane protein
Phosphatidylserine decarboxylase alpha chain
Mitochondrion inner membrane ; Peripheral membrane protein
Note: Anchored to the mitochondrial inner membrane through its interaction with the integral membrane beta chain.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 50-60 | Mitochondrial matrix | ||||
Sequence: VHTAPLRTLFL | ||||||
Transmembrane | 61-79 | Helical | ||||
Sequence: LRPVPILLAAGGGYAGYRQ | ||||||
Topological domain | 80-406 | Mitochondrial intermembrane | ||||
Sequence: YEKYRERQLEKLGLEIPPKLASHWEVSLYKSVPTRLLSRACGRLNQVELPSWLRRPVYSLYIWTFGVNMTEAAVEDLQHYRNLSEFFRRKLKPQARPVCGLHSVISPSDGKILTFGQVKNSEVEQVKGVTYSLESFLGPRACTEDLPFPPASSCDSFRNQLVTREGNELYHCVIYLAPGDYHCFHSPTDWTVSHRRHFPGSLMSVNPGMARWIKELFCHNERVVLTGDWKHGFFSLTAVGATNVGSIRIHFDQDLHTNSPSYSKGSYNDLSFVTHANKEGIPMRKGEPLGEFNLGSTIVLIFEAPKDFNFRLKAGQKILFGEALGSL |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-49 | Mitochondrion | ||||
Sequence: MAVAGGRGCVRSLREGVLWRSSPCHCDYTATRHFLGALQKLPLQAWVRK | ||||||
Chain | PRO_0000435575 | 50-374 | Phosphatidylserine decarboxylase beta chain | |||
Sequence: VHTAPLRTLFLLRPVPILLAAGGGYAGYRQYEKYRERQLEKLGLEIPPKLASHWEVSLYKSVPTRLLSRACGRLNQVELPSWLRRPVYSLYIWTFGVNMTEAAVEDLQHYRNLSEFFRRKLKPQARPVCGLHSVISPSDGKILTFGQVKNSEVEQVKGVTYSLESFLGPRACTEDLPFPPASSCDSFRNQLVTREGNELYHCVIYLAPGDYHCFHSPTDWTVSHRRHFPGSLMSVNPGMARWIKELFCHNERVVLTGDWKHGFFSLTAVGATNVGSIRIHFDQDLHTNSPSYSKGSYNDLSFVTHANKEGIPMRKGEPLGEFNLG | ||||||
Chain | PRO_0000435574 | 50-406 | Phosphatidylserine decarboxylase proenzyme, mitochondrial | |||
Sequence: VHTAPLRTLFLLRPVPILLAAGGGYAGYRQYEKYRERQLEKLGLEIPPKLASHWEVSLYKSVPTRLLSRACGRLNQVELPSWLRRPVYSLYIWTFGVNMTEAAVEDLQHYRNLSEFFRRKLKPQARPVCGLHSVISPSDGKILTFGQVKNSEVEQVKGVTYSLESFLGPRACTEDLPFPPASSCDSFRNQLVTREGNELYHCVIYLAPGDYHCFHSPTDWTVSHRRHFPGSLMSVNPGMARWIKELFCHNERVVLTGDWKHGFFSLTAVGATNVGSIRIHFDQDLHTNSPSYSKGSYNDLSFVTHANKEGIPMRKGEPLGEFNLGSTIVLIFEAPKDFNFRLKAGQKILFGEALGSL | ||||||
Modified residue | 375 | Pyruvic acid (Ser); by autocatalysis | ||||
Sequence: S | ||||||
Chain | PRO_0000435576 | 375-406 | Phosphatidylserine decarboxylase alpha chain | |||
Sequence: STIVLIFEAPKDFNFRLKAGQKILFGEALGSL |
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
Expression
Gene expression databases
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. Eukaryotic type I sub-subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length406
- Mass (Da)45,824
- Last updated2015-07-22 v3
- Checksum5358A6A2A6D72EE7
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0G2JTF7 | A0A0G2JTF7_RAT | Pisd | 375 | ||
A0A0G2K0F9 | A0A0G2K0F9_RAT | Pisd | 262 | ||
A0A8I6GLT0 | A0A8I6GLT0_RAT | Pisd | 409 | ||
A0A8I5ZNJ4 | A0A8I5ZNJ4_RAT | Pisd | 365 | ||
A0A8L2QDB1 | A0A8L2QDB1_RAT | Pisd | 388 |
Keywords
- Technical term