A0A5A7MGS8 · A0A5A7MGS8_COMTE

Function

function

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

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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 site76Charge relay system; for autoendoproteolytic cleavage activity
Active site133Charge relay system; for autoendoproteolytic cleavage activity
Site236-237Cleavage (non-hydrolytic); by autocatalysis
Active site237Charge relay system; for autoendoproteolytic cleavage activity
Active site237Schiff-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
    • ORF names
      CTTA_2880

Organism names

Accessions

  • Primary accession
    A0A5A7MGS8

Proteomes

Subcellular Location

Cell membrane
; Peripheral membrane protein

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_50235582381-236Phosphatidylserine decarboxylase beta chain
Modified residue237Pyruvic acid (Ser); by autocatalysis
ChainPRO_5023558237237-275Phosphatidylserine 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.

Family & Domains

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    275
  • Mass (Da)
    29,688
  • Last updated
    2019-11-13 v1
  • MD5 Checksum
    8388A179A84AD90B47534A4C72737D04
MPKQALTALMGKLAQAEVGGLTTAVIRRFIQRYQVNMAEAANPDPAAYKTFNAFFTRALKDGVRPLAQADWICPVDGAISQFGRIEGEQIFQAKGHQYSATALVGGDAALARQFDNGSFATIYLSPRDYHRIHMPCAGKLRSMTYVPGDLFSVNPVTARGVPGLFARNERVVCVFDTDHGPFVLVLVGATIVGSMATVWHGLVNPPRPGHIKTWNYEGAEAVTLASGEEMGRFQLGSTVVMLFPQAAGLQFNPQWQPAAPVQLGQVMGNAQIKLG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BKBW01000004
EMBL· GenBank· DDBJ
GEQ75875.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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