A0A8H4MYR4 · A0A8H4MYR4_9PEZI

  • 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

Lacks conserved residue(s) required for the propagation of feature annotation.
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 site252Charge relay system; for autoendoproteolytic cleavage activity
Site379-380Cleavage (non-hydrolytic); by autocatalysis
Active site380Charge relay system; for autoendoproteolytic cleavage activity
Active site380Schiff-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
      GTA08_BOTSDO11518

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • sdau11-99
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Dothideomycetes > Dothideomycetes incertae sedis > Botryosphaeriales > Botryosphaeriaceae > Botryosphaeria

Accessions

  • Primary accession
    A0A8H4MYR4

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 domain1-7Mitochondrial matrix
Topological domain23-430Mitochondrial intermembrane

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_50350320601-379Phosphatidylserine decarboxylase 1 beta chain
Modified residue380Pyruvic acid (Ser); by autocatalysis
ChainPRO_5035032059380-430Phosphatidylserine 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 bias1-27Basic and acidic residues
Region1-32Disordered
Compositional bias129-157Polar residues
Region129-168Disordered

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    430
  • Mass (Da)
    48,352
  • Last updated
    2022-01-19 v1
  • Checksum
    22CCB67B8BDDF475
MKRPGETTRRARTGVVDNGDGERPRKRKRIRPSGPWQVQVMSTLPLKALSRLWGRFNELDIPYYLRVPGFRLYSFIFGVNLDEMEEQDLHKYPNLAKFFYRTLKPGFGTIDNGEVEQVKGVTYSLDALLGSNPPSRRSSDAGSNISSSPSSPQPSSERKAMETKKSSRLTRSLVVSMVFPIRYPISSQAHPRARRARSWISPTPHSASAEAEVRADLELGQRPWWSPMTTPKAHCLYYCVIYLAPGDYHRFHSPVSWVTESRRHFAGELYSVSPYLVRTLPGLFTLNERVVLLGRWRWGFFSYIPVGATNVGSIVINFDRELRTNSLTTDTAADRAAEEAQRRGEPYSGYAEATYYGASNVLGGHALKKGEEMGGFQLGSTIVLVFEAPKPQRKSSLDEGFTGTKGGWKWNIEKGQKLKVGQAIGYVEED

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-27Basic and acidic residues
Compositional bias129-157Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
WWBZ02000082
EMBL· GenBank· DDBJ
KAF4300703.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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