S3CCK9 · S3CCK9_OPHP1

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 site247Charge relay system; for autoendoproteolytic cleavage activity
Active site397Charge 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 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
      F503_07477

Organism names

Accessions

  • Primary accession
    S3CCK9

Proteomes

Organism-specific databases

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.

TypeIDPosition(s)Description
Topological domain1-107Mitochondrial matrix
Topological domain127-579Mitochondrial intermembrane

Keywords

PTM/Processing

Features

Showing features for signal, chain, modified residue.

TypeIDPosition(s)Description
Signal1-23
ChainPRO_50232316861-524Phosphatidylserine decarboxylase 1 beta chain
ChainPRO_500451845724-579Phosphatidylserine decarboxylase proenzyme 1, mitochondrial
Modified residue525Pyruvic acid (Ser); by autocatalysis
ChainPRO_5023231687525-579Phosphatidylserine 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 region.

TypeIDPosition(s)Description
Region132-159Disordered
Region333-356Disordered

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    579
  • Mass (Da)
    63,579
  • Last updated
    2013-09-18 v1
  • Checksum
    24A46C96B087C858
MLFLLFILGLVVLTLLLVAPTPAGIRMASAPSRLGLSRGSFSKGITTGRFSVSLSERQILFNPPRRLVLNSSPFRFYSPFRFYSQQAARRPRFSARLRQAIKNSKVQWYRIPVGLGIGFLGVVQLYKSRNRKATPEDGTDAATDAASKPPKRPRIRPDGPWQIQVMSTLPLKALSRLWGRFNELTLPYYLRVPGFKLYSYAFGVNLDEVEEPDLHNFPNLSSFFYRTLKPGVRPIDPHHSALTSPSDGKIIQFGKIEGGDIEQVKGMTYSLDALLGKHTPAPSIASGMTSSSASSTATLIPSKREGDEQLVRADEDFAKVNGISYTLPGLISGPDVTDRAEEDLEDQSAQPSLPKSVSEVQADLDSPWYTQLLSRDKKTSLYYAVIYLAPGDYHRFHSPTNWVVERRRHFAGELYSVSPYLQRTLPGLFTLNERVVLLGRWKWGFFSYIPVGATNVGSIIVNFDRELRTNSLTTDTAADRAAAEAAARGEAYSGFAEATYASASPTLHGHALERGEEMGGFQLGSTVVLVFEAPTPEAASAAAPGAGGAVDPKSTPGWHWAVEKGQKIKMGQALGFVNE

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KE148147
EMBL· GenBank· DDBJ
EPE09701.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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