G2YCZ4 · G2YCZ4_BOTF4

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 site229Charge relay system; for autoendoproteolytic cleavage activity
Active site384Charge relay system; for autoendoproteolytic cleavage activity
Site511-512Cleavage (non-hydrolytic); by autocatalysis
Active site512Charge relay system; for autoendoproteolytic cleavage activity
Active site512Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity

GO annotations

AspectTerm
Cellular Componentmitochondrial inner membrane
Molecular Functionphosphatidylserine decarboxylase activity
Biological Processphosphatidylethanolamine biosynthetic process
Biological Processprotein autoprocessing

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • Name
      PSD1
    • ORF names
      BofuT4_P097500.1

Organism names

Accessions

  • Primary accession
    G2YCZ4

Proteomes

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, transmembrane.

TypeIDPosition(s)Description
Topological domain1-77Mitochondrial matrix
Transmembrane74-94Helical
Topological domain97-563Mitochondrial intermembrane

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_50235044261-511Phosphatidylserine decarboxylase 1 beta chain
Modified residue512Pyruvic acid (Ser); by autocatalysis
ChainPRO_5023504427512-563Phosphatidylserine 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 compositional bias, region.

TypeIDPosition(s)Description
Compositional bias100-115Basic and acidic residues
Region100-139Disordered
Compositional bias125-139Basic and acidic residues
Compositional bias259-283Polar residues
Region259-291Disordered
Compositional bias315-338Polar residues
Region315-344Disordered

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    563
  • Mass (Da)
    62,981
  • Last updated
    2011-11-16 v1
  • Checksum
    9BC532D961C2C682
MAYRLVAAHATPSQSSQRGLHTLRTSSILGQSQCICRCHRPRNFSSSARFYRQNNDYKESFGTRLRRALNDTKITWYHIPVGLGIAFLGLGQIYRVNEREKARRREEDEDGFVRSVGSGDDGNDEGYQGRPKRRERVRPSGPWQVQVMSTLPLKAMSRIWGRFNELEIPYYLRVPGFKLYSFIFGVNLSEVSEPDLHVYPNLASFFYRTLKPGARPLHPNPNALLSPSDGRVLQFGAIESGEVEQVKGMTYSLDALLGTSKPATTPNPADPSNIFTPPQDTIPKQSKARYKDGDEEIIKQDEKFATVNGISYTLPNLLSGPPQKQPGKKSSDASTTPKAASEAEVRADLALGEKPWYSRVTTENKTALYYVVVYLAPGDYHRFHSPTAWVAEKRRHFAGELYSVSPYLQRTLPGLFTLNERVVLLGRWRWGFFSFIPVGATNVGSIKINFDRELRTNSLTTDTAADRAAAEAAERGESYSGFAEATYEAASPILHGHALRRGEEMGGFQLGSTVVLVFEAPKGTRPSLDEGWMGQKRKGGWNWAIEKGQRVKMGEQLGWVDDA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias100-115Basic and acidic residues
Compositional bias125-139Basic and acidic residues
Compositional bias259-283Polar residues
Compositional bias315-338Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FQ790320
EMBL· GenBank· DDBJ
CCD49642.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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