A0A1S9RQF8 · A0A1S9RQF8_PENBI

  • Protein
    Phosphatidylserine decarboxylase proenzyme 1, mitochondrial
  • Gene
    psd1
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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.

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.

TypeIDPosition(s)Description
Active site223Charge relay system; for autoendoproteolytic cleavage activity
Active site367Charge relay system; for autoendoproteolytic cleavage activity
Site494-495Cleavage (non-hydrolytic); by autocatalysis
Active site495Charge relay system; for autoendoproteolytic cleavage activity
Active site495Schiff-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
    • Synonyms
      PSD1
    • ORF names
      PEBR_16393

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • LaBioMMi 136
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Penicillium

Accessions

  • Primary accession
    A0A1S9RQF8

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.

TypeIDPosition(s)Description
Topological domain1-83Mitochondrial matrix
Topological domain103-546Mitochondrial intermembrane

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_50233863321-494Phosphatidylserine decarboxylase 1 beta chain
Modified residue495Pyruvic acid (Ser); by autocatalysis
ChainPRO_5023386333495-546Phosphatidylserine 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.

Family & Domains

Features

Showing features for compositional bias, region.

TypeIDPosition(s)Description
Compositional bias108-127Basic and acidic residues
Region108-133Disordered
Region303-326Disordered

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    546
  • Mass (Da)
    60,807
  • Last updated
    2017-05-10 v1
  • Checksum
    6F4315CA70DDCC8E
MAKRLLNHSTFLQCRAAAPVSGVATSMEVLSFRATARHKASVRQFSSKSWKQYQKENNHEGKARGGFGSRLRFALRNTKVEWYPIPVGLGIGLLGVLHFYKSQRAERDRNAQDEAGDAWENGKRPPRRPRVVPTGPWQVQVMSTLPLKAISRLWGRFNEIELPYYFRVPGFKLYSWVFGVNLSEVAEPDLHVYPNLAAFFYRKLKPGVRPLDPDPRALVSPSDGRILQFGMIERGEVEQVKGMTYSLDALLGAATPVTADHSNRMSDPAIKDTHKDVENMKADEEFASVNGISYTLPSLLSGESGAPAKRRASIDASTPSKTTSEVQVQEELARGEGTSWFASKEAVNHALFYVVIYLAPGDYHRFHSPTEWVVESRRHFAGELYSVSPYLQRTLPGLFTLNERVALLGRWRWGFFSYIPVGATNVGSIKINFDSELRTNSLLTDTAADLAAARAAERGETDPGFVEATYAHASRTLGGHPLRRGEEMGGFQLGSTVVLVFEAPLGGRKSFDAGWPDKERPDGWNWAIEKGQRIKMGEKLGFVGED

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias108-127Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LJBN01000123
EMBL· GenBank· DDBJ
OOQ87757.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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