A0A7C8YEX9 · A0A7C8YEX9_OPUST

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.

TypeIDPosition(s)Description
Active site381Charge relay system; for autoendoproteolytic cleavage activity
Active site437Charge relay system; for autoendoproteolytic cleavage activity
Site524-525Cleavage (non-hydrolytic); by autocatalysis
Active site525Charge relay system; for autoendoproteolytic cleavage activity
Active site525Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity

GO annotations

AspectTerm
Cellular Componentmembrane
Molecular Functioncalcium ion binding
Molecular Functionphosphatidylserine decarboxylase activity
Biological Processphosphatidylethanolamine biosynthetic process
Biological Processprotein autoprocessing

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • Name
      PSD2

Organism names

Accessions

  • Primary accession
    A0A7C8YEX9

Subcellular Location

Keywords

  • Cellular component

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_50285403451-524Phosphatidylserine decarboxylase 2 beta chain
Modified residue525Pyruvic acid (Ser); by autocatalysis
ChainPRO_5028540346525-570Phosphatidylserine decarboxylase 2 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.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-84C2
Domain112-147EF-hand
Domain148-183EF-hand

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    570
  • Mass (Da)
    63,727
  • Last updated
    2020-12-02 v1
  • Checksum
    2A91846E4400678D
MKFKDKWMACVSLGEQTFRTNISDHTDKPVWNSEKKILLESNGPHVARVSIYETNLLTKNNLIGFCEIDLFQFLAQDSDSDFETVDLLDPSSSDTVVGKLSFSCFVEDPQETEKGFARRLLSIMDYNEDGQLSFSEFSDLVDAFGNQVASDKKEELFKAADENGDGVVSMDELASLLARHQEKEPLINSCPVCGEVLEASNRLGSMIHMTLCFNEGTGNHVMSGGFLTDKQASYGWLFKLSEWTHVSSYGIGLHSGSQSAHILVFDRTQKRLVEELIDGKIILSMRAIYQSRLGLQLMDKGAKEILQELSEKQGKKMNSVDSAKDIPKFINFFQDQINVSEMKYPLDHFKTFNEFFIRELKPGVRPIACMDRDDVAVCAADSRLMAFKTVEESTRFWIKGRKFSIEGLLGKDISSSPFIDGTLVIFRLAPQDYHRFHLPVSGTVEQFVDIAGSLYTVNPIAVNSKYCNVFTENKRTVAIISTADFGKVAFVAIGATMVGSITFTKEEGDYVKKGDEFGYFSFGGSTVICVFQKDVIRLDDDLLENSARSLETLVRVGMRLGISTKADIQS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GISG01011297
EMBL· GenBank· DDBJ
MBA4616435.1
EMBL· GenBank· DDBJ
Transcribed RNA

Similar Proteins

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