S0EBK4 · S0EBK4_GIBF5

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.

Catalytic activity

Cofactor

pyruvate (UniProtKB | Rhea| CHEBI:15361 )

Note: Binds 1 pyruvoyl group covalently per subunit.

Pathway

Lipid metabolism.
Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.

Features

Showing features for active site, site.

Type
IDPosition(s)Description
Active site225Charge relay system; for autoendoproteolytic cleavage activity
Active site369Charge relay system; for autoendoproteolytic cleavage activity
Site496-497Cleavage (non-hydrolytic); by autocatalysis
Active site497Charge relay system; for autoendoproteolytic cleavage activity
Active site497Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity

GO annotations

AspectTerm
Cellular Componentendoplasmic reticulum membrane
Cellular Componentmitochondrial inner membrane
Molecular Functionphosphatidylserine decarboxylase activity
Biological Processlipid droplet formation
Biological Processmitochondrial electron transport, ubiquinol to cytochrome c
Biological Processphosphatidylcholine biosynthetic process
Biological Processphosphatidylethanolamine biosynthetic process
Biological Processpositive regulation of mitochondrial fusion
Biological Processpositive regulation of protein processing
Biological Processprotein autoprocessing

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • Name
      PSD1
    • ORF names
      FFUJ_12181

Organism names

Accessions

  • Primary accession
    S0EBK4

Proteomes

Organism-specific databases

Subcellular Location

Phosphatidylserine decarboxylase 1 alpha chain

Mitochondrion inner membrane
; Peripheral membrane protein
Note: Anchored to the mitochondrial inner membrane through its interaction with the integral membrane beta chain.

Phosphatidylserine decarboxylase 1 beta chain

Mitochondrion inner membrane
; Single-pass membrane protein

Features

Showing features for topological domain.

TypeIDPosition(s)Description
Topological domain1-88Mitochondrial matrix
Topological domain108-540Mitochondrial intermembrane

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_50232853211-496Phosphatidylserine decarboxylase 1 beta chain
Modified residue497Pyruvic acid (Ser); by autocatalysis
ChainPRO_5023285323497-540Phosphatidylserine decarboxylase 1 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 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

Interaction

Subunit

Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region113-133Disordered
Region260-280Disordered

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    540
  • Mass (Da)
    60,044
  • Last updated
    2013-09-18 v1
  • Checksum
    7A6B60643EA081F2
MAPTLGFGPGSSKLGSHMLRNSFYTHGRWTNCYSPSASRHMFLASTRSRCLSRPSVSSIRTFASNSGKRPRFSQRLGEAMRNTKIQWYRIPVGLGIGFLGLVQFYKVSSREKERLDNEDGQEGSRAPKKRARIRPDGPWQVQVMSTLPLKAISRLWGRFNELTIPYYLRVPGFKLYSWIFGVNLDEVAEPDLHVYPNLASFFYRTLKPGARPLDQDPHTLICPSDGKVLQFGQIQGNDIEQVKGMTYTIDALLGKNTPAPSISGASGTSTPATSQGDVSEEESLVKQHEEFAQVNGISYTLPDLLTGTGKQAPSAKDESMPASPGTVSEVRAELALGERPWYDLISPDNTTSLYYAVIYLAPGDYHRFHSPTNWVVDRRRHFAGELYSVSPYLQRTLPGLFTLNERVVLLGRWRWGFFSYVPVGATNVGSIVINFDKELRTNSLLTDTAADRAAEEAAHRGEVYHGFAEATYEAASPVLRGHALRRGEEMGGFQLGSTIVLVFEAPSGKTDENNRHVGWDWAVQKGQKVKMGQALGRVIE

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
HF679030
EMBL· GenBank· DDBJ
CCT72326.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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