A1VUQ1 · PSD_POLNA

Function

function

Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).

Catalytic activity

Cofactor

pyruvate (UniProtKB | Rhea| CHEBI:15361 )

Note: Binds 1 pyruvoyl group covalently per subunit.

Pathway

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

Features

Showing features for active site, site.

TypeIDPosition(s)Description
Active site88Charge relay system; for autoendoproteolytic cleavage activity
Active site145Charge relay system; for autoendoproteolytic cleavage activity
Site250-251Cleavage (non-hydrolytic); by autocatalysis
Active site251Charge relay system; for autoendoproteolytic cleavage activity
Active site251Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity

GO annotations

AspectTerm
Cellular Componentplasma membrane
Molecular Functionphosphatidylserine decarboxylase activity
Biological Processphosphatidylethanolamine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • Name
      psd
    • Ordered locus names
      Pnap_4088

Organism names

Accessions

  • Primary accession
    A1VUQ1

Proteomes

Subcellular Location

Cell membrane
; Peripheral membrane protein

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_10000265621-250Phosphatidylserine decarboxylase beta chain
Modified residue251Pyruvic acid (Ser); by autocatalysis
ChainPRO_1000026563251-289Phosphatidylserine 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 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

Structure

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    289
  • Mass (Da)
    31,778
  • Last updated
    2007-02-06 v1
  • Checksum
    747F000D5EBED966
MSDRLAVLPQYLLPKQALTHFAGFVASRERGWVTTEIIRRFVAKYRVNMSEALDSDIASYLTFNDFFTRALKPGARPLAQAALVCPVDGAISQFGAIEHDQIFQAKGHHYSTTALVGGDAALAAHYQNGHFATIYLSPKDYHRIHMPCDGRLTRMIYVPGDLFSVNPVTARGVPGLFARNERVVCVFESARGPFVLALVGATIVGSMATVWHGVVNPPRGKAVREWRYPASGQPEVVLRQGEEMGRFLLGSTVVLLFPKGPLRFNPDWEPGRAVRLGEAMADVAADSQR

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000529
EMBL· GenBank· DDBJ
ABM39379.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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