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The annotation and conditions in this rule are derived from the following entries: Q9FDI9 (PSD_RHIME), O28234 (ASD_ARCFU), P0A8K1 (PSD_ECOLI)

If a protein meets these conditions... i

Common conditions

Special conditions

    • Subsequence at position 189 - 190 aligns to "G-S" in entry Q9FDI9 (individually applies "Cleavage (non-hydrolytic); by autocatalysis")
    • Subsequence at position 190 - 190 aligns to "S" in entry Q9FDI9 (individually applies "Schiff-base intermediate with substrate; via pyruvic acid")
    • Subsequence at position 190 - 190 aligns to "S" in entry Q9FDI9 (individually applies "Pyruvic acid (Ser); by autocatalysis")

... then these annotations are applied i

Protein namesi

  • Recommended name:
    Putative archaetidylserine decarboxylase proenzyme (EC:4.1.1.-)
  • Recommended name:
    Phosphatidylserine decarboxylase proenzyme (EC:4.1.1.65)

Cleaved chain(s) or included domain(s)i

  • Cleaved chain:
    Recommended name:
    Archaetidylserine decarboxylase beta chain
  • Cleaved chain:
    Recommended name:
    Archaetidylserine decarboxylase alpha chain
  • Cleaved chain:
    Recommended name:
    Phosphatidylserine decarboxylase beta chain
  • Cleaved chain:
    Recommended name:
    Phosphatidylserine decarboxylase alpha chain

Gene namesi

  • Name:asd
  • Name:psd

Subunit structurei

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

Pathwayi

  • Pathwayi: phosphatidylethanolamine biosynthesis

    This protein is involved in step 2 of the subpathway that synthesizes phosphatidylethanolamine from CDP-diacylglycerol. This subpathway is part of the pathway phosphatidylethanolamine biosynthesis, which is itself part of Phospholipid metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes phosphatidylethanolamine from CDP-diacylglycerol, the pathway phosphatidylethanolamine biosynthesis and in Phospholipid metabolism.

Functioni

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

Catalytic activityi

  • Archaetidyl-L-serine = Archaetidylethanolamine + CO2.
  • Phosphatidyl-L-serine = phosphatidylethanolamine + CO2.

Post-translational modificationi

  • 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 post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, 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.

Subcellular locationi

Cofactori

  • pyruvateNote: Binds 1 pyruvoyl group covalently per subunit.

Sequence similaritiesi

Modified residuei

  • Pyruvic acid (Ser); by autocatalysis (to residues corresponding to position 190)

Active sitei

  • Schiff-base intermediate with substrate; via pyruvic acid (to residues corresponding to position 190)

Sitei

  • Cleavage (non-hydrolytic); by autocatalysis (to residues corresponding to positions 189 - 190)

Keywordsi

GO (Gene Ontology) termsi