A0A317XI57 · A0A317XI57_9BASI

  • 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.

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 site348Charge relay system; for autoendoproteolytic cleavage activity
Active site558Charge relay system; for autoendoproteolytic cleavage activity
Site671-672Cleavage (non-hydrolytic); by autocatalysis
Active site672Charge relay system; for autoendoproteolytic cleavage activity
Active site672Schiff-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
      BCV70DRAFT_166937

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • MCA 3645
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Basidiomycota > Ustilaginomycotina > Ustilaginomycetes > Ustilaginales > Anthracoideaceae > Testicularia

Accessions

  • Primary accession
    A0A317XI57

Proteomes

Subcellular Location

Membrane

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.

Type
IDPosition(s)Description
Topological domain1-215Mitochondrial matrix
Transmembrane7-25Helical
Transmembrane31-54Helical
Transmembrane214-233Helical
Topological domain235-720Mitochondrial intermembrane

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_50232942371-671Phosphatidylserine decarboxylase 1 beta chain
Modified residue672Pyruvic acid (Ser); by autocatalysis
ChainPRO_5023294239672-720Phosphatidylserine 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, compositional bias.

Type
IDPosition(s)Description
Region165-200Disordered
Region382-404Disordered
Compositional bias383-404Basic and acidic residues
Region418-440Disordered
Compositional bias458-481Polar residues
Region458-497Disordered

Sequence similarities

Belongs to the UPF0057 (PMP3) family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    720
  • Mass (Da)
    80,110
  • Last updated
    2018-10-10 v1
  • Checksum
    D129C088A9D1BDD2
MAGGADIILILVALIFPPAAVAFITGCSCDLMINILLTVLGYLPGHIHAFWLIYKKMKAEERYGDAIQYTGNGEWVPKHGQPIYQPPPPAYGATHTSLSLSLRSRQQLLSLQRHGLAGSYRARHLQTISQTSRPQIRIRDRKPIPPLQLRLLPSPRHYSRDPLQAEHEANTVRGHRSARLRSEKEARKSPEDQSDSNDRSYREKLSRSWFGTQVKWYPIPILLGAVVLVGVQARRNYVAERDGKGVGNKIVDENGQVVKMQGPWTVYVIGALPLNAISRAWGWANNITLPIWFRPFGFKLYASIFGCNLDEMKDPDLTHYKSLGEFFYRELKDGARPIDDSVLVSPADGKVLHFGEIMGRRVEQVKGITYSLDALLGVTSEPEATEKVERGQAGDHERLDDRQFASVNGIEYSLDELLGDKKSRSAPPPPDAEKPKQSMKRFVKPSYWKSWFVRSKPDGTNTTDIPPSVSGDRSAANDNKNDAGASGGPKEPMDDAGIAEPDTPEVLGRYANVAYEMGVGALPPLLQPHSPGAKGIRDGNKLFFCVVYLAPGDYHRFHSPTNWVAERRRHFRGELYSVSPYMANRLSNLFVLNERVALLGRWRHGFFGMVPVGATNVGSIRINFDKALRTNVRKQRYLAGTYSEASYAGASKLLGGQPLGAGDEMGGFLLGSTIVLVFEAPADFRFDLHPGQKIKVGERMGDVRPQVHIEEEEKKNGRVV

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias383-404Basic and acidic residues
Compositional bias458-481Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KZ819207
EMBL· GenBank· DDBJ
PWY97487.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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